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Information on EC 1.1.1.27 - L-lactate dehydrogenase
for references in articles please use BRENDA:EC1.1.1.27
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.27 L-lactate dehydrogenase
IUBMB Comments
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 1.1.1.27
- creatine
- aminotransferase
- myocardial
- isoenzymes
- cardiac
- dismutase
- necrosis
- malondialdehyde
- ischemia
- albumin
- catalase
- lymphoma
- infarct
- transaminase
-
reperfusion
- lymphocyte
- platelet
- sod
- artery
-
alt
- pulmonary
- hemoglobin
-
c-reactive
- hepatocytes
- coronary
- wistar
- bilirubin
- gsh
- hypoxia
- caspase-3
-
cardioprotective
- ventricular
- fever
-
admission
- covid-19
-
admitted
-
cardiomyocytes
-
ischemia-reperfusion
-
phosphokinase
-
hepatotoxicity
- troponin
-
progression-free
-
bronchoalveolar
- chest
-
hemolysis
-
trypan
-
uric
-
non-hodgkin
- coronavirus
-
d-dimer
- medicine
- degradation
- diagnostics
- biotechnology
- analysis
- drug development
- synthesis
- agriculture
showSynonyms
lactate dehydrogenase, lactic dehydrogenase, ldh-a, lactate dehydrogenase a, l-lactate dehydrogenase, ldh-5, lactic acid dehydrogenase, ldh-1, pfldh, alpha-hydroxybutyrate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A4-LDH
AdhE
anaerobic lactate dehydrogenase
dehydrogenase, lactate
-
-
-
-
Epsilon crystallin
-
-
-
-
epsilon-crystallin
-
-
-
-
Immunogenic protein p36
-
-
-
-
L(+)-nLDH
-
-
-
-
L-(+)-lactate dehydrogenase
L-lactic acid dehydrogenase
-
-
-
-
L-lactic dehydrogenase
-
-
-
-
L-LDH
L-nLDH
lactate dehydrogenase
lactate dehydrogenase A
lactate dehydrogenase B
lactate dehydrogenase NAD-dependent
-
-
-
-
lactic acid dehydrogenase
-
-
-
-
lactic dehydrogenase
-
-
-
-
LctD
LDH
LDH-1
LDH-2
LDH-5
LDH-A
LDH1
LDH2
LdhA
LDHB
ldhL
LDHL1
LDHL2
LutACB
NAD-dependent lactate dehydrogenase
NAD-lactate dehydrogenase
-
-
-
-
NGO0904
NGO0905
NGO0906
PfLDH
proteins, specific or class, anoxic stress response, p34
-
-
-
-
SMU_1115
TeLdhL
Tsac_0416
additional information
-
lactate dehydrogenase is a member of the 2-hydroxyacid oxidoreductase family
AdhE
bifunctional alcohol and aldehyde dehydrogenase gene
AdhE
bifunctional alcohol and aldehyde dehydrogenase gene
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L-(+)-lactate dehydrogenase
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-
-
-
L-LDH
-
-
-
-
lactate dehydrogenase
-
-
-
-
LDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-lactate + NAD+ = pyruvate + NADH + H+
reduction of pyruvate follows an Theorell-Chance mechanism
-
(S)-lactate + NAD+ = pyruvate + NADH + H+
the NAD (H)-dependent L-LDH catalyzes the reduction of pyruvate by an ordered catalytic mechanism, catalytic cycle, overview
-
(S)-lactate + NAD+ = pyruvate + NADH + H+
the enzyme-NADH-pyruvate ternery complex undergoes a rate-limiting conformational change, in which the substrate loop closes to form a desolvated ternary complex in order to bring the catalytic residue Arg109 into the active site, the catalytic residues Arg109, Asp168, and His195 are highly conserved, catalyic mechanism, detailed overview
-
(S)-lactate + NAD+ = pyruvate + NADH + H+
the enzyme LDHA shows an ordered bibi kinetic mechanism of nLDH with the coenzyme binding first
-
(S)-lactate + NAD+ = pyruvate + NADH + H+
the enzyme LDHA shows an ordered bibi kinetic mechanism of nLDH with the coenzyme binding first
Lactococcus cremoris MG1363
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-
(S)-lactate + NAD+ = pyruvate + NADH + H+
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
redox reaction
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-
-
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reduction
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
(S)-lactate fermentation to propanoate, acetate and hydrogen, Bifidobacterium shunt, heterolactic fermentation, L-histidine degradation V, pyruvate fermentation to (S)-lactate, superpathway of glucose and xylose degradation
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SYSTEMATIC NAME
IUBMB Comments
(S)-lactate:NAD+ oxidoreductase
Also oxidizes other (S)-2-hydroxymonocarboxylic acids. NADP+ also acts, more slowly, with the animal, but not the bacterial, enzyme.
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CAS REGISTRY NUMBER
COMMENTARY
9001-60-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-lactate + 3-acetyl pyridine adenine dinucleotide
pyruvate + reduced 3-acetyl pyridine adenine dinucleotide
-
Substrates: assay is based on reduction of 3-acetyl pyridine adenine dinucleotide that is specific for PfLDH, which allows the distinction of PfLDH from that of the host erythrocyte
Products: -
Products: -
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
(S)-lactate + APAD+
pyruvate + APADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + epsilon-NAD+
pyruvate + epsilon-NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NADP+
pyruvate + NADPH + H+
Substrates: wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active with NADP+
Products: -
Products: -
?
(S)-lactate + nicotinamide hypoxanthine dinucleotide
pyruvate + reduced nicotinamide hypoxanthine dinucleotide
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
Substrates: -
Products: -
Products: -
?
2-oxopentanoate + NADH
2-hydroxypentanoate + NAD+
-
Substrates: 125% of the activity with pyruvate
Products: -
Products: -
?
2-oxovalerate + NADH
2-hydroxyvalerate + NAD+
-
Substrates: -
Products: -
Products: -
r
3,4-dihydroxyphenylpyruvate + NADH + H+
L-3,4-dihydroxyphenyllactate + NAD+
Substrates: 8.5% of the activity with pyruvate
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH
2-hydroxy-3-methylbutanoate + NAD+
-
Substrates: 28.5% of the activity with pyruvate
Products: -
Products: -
?
3-methyl-2-oxopentanoate + NADH
2-hydroxy-3-methylpentanoate + NAD+
-
Substrates: 5.3% of the activity with pyruvate
Products: -
Products: -
?
4-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-4-methylpentanoate + NAD+
Substrates: 25.9% of the activity with pyruvate
Products: -
Products: -
?
benzoylformate + NADH + H+
L-hydroxy(phenyl)acetate + NAD+
Substrates: 20.5% of the activity with pyruvate
Products: -
Products: -
?
benzoylformic acid + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
bromopyruvate + NADH
3-bromo-2-hydroxypropanoate + NAD+
-
Substrates: -
Products: -
Products: -
?
ethyl pyruvate + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
methyl pyruvate + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADH + H+
? + NAD+
Substrates: -
Products: -
Products: -
?
oxamate + NADH
?
-
Substrates: two distinct active site LDH/NADH-oxamate complex conformations, a major populated structure wherein all significant hydrogen-bonding patterns are formed at the active site between protein and bound ligand necessary for the catalytically productive Michaelis complex and, a minor structure in a configuration of the active site that is unfavorable to carry out catalyzed chemistry. This latter structure likely simulates a dead-end complex in the reaction mixture. The evolution of the encounter complex between LDH/NADH and oxamate collapses via a branched reaction pathway to form the major and minor bound species. Once the encounter complex is formed between LDH/NADH and substrate, the ternary protein-ligand complex appears to fold to form a compact productive complex in an all or nothing like fashion with all the important molecular interactions coming together at the same time
Products: -
Products: -
?
pyruvate + APADH + H+
(S)-lactate + APAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADPH + H+
L-lactate + NADP+
Substrates: -
Products: -
Products: -
?
pyruvate ethyl ester + NADH
2-hydroxypropanoate ethyl ester
-
Substrates: -
Products: -
Products: -
?
pyruvate methyl ester + NADH
2-hydroxypropanoate methyl ester
-
Substrates: -
Products: -
Products: -
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
Substrates: -
Products: -
Products: -
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
(S)-lactate + 3-acetylpyridine adenine dinucleotide
pyruvate + reduced 3-acetylpyridine adenine dinucleotide
Substrates: -
Products: -
Products: -
?
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
Substrates: L-lactate transport and metabolism, regulation and localization of enzyme participating in the pathway, overview
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: mutant I12V/R81Q/M85E/G210A/V214I, residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active with NADP+
Products: -
Products: -
?
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: residues I12, R81, M85, G210, and V214 determine the enzyme's substrate specificity
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: the astrocytic cell line CCF-STTG1 is able to consume lactate to generate ATP via oxidative phosphorylation, overview
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: since the mitochondrial metabolism of (S)-lactate results in synthesis and export of oxaloacetate, malate and citrate into the extramitochondrial phase, an anaplerotic role for the mitochondrial (S)-lactate metabolism is proposed
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: the maximal velocity of lactate oxidation is about 10% of pyruvate reduction
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Lactococcus cremoris MG1363
-
Substrates: lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: inactive towards D-lactate
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: LDH posseses a catalytic His171 residue
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: LDH posseses a catalytic His171 residue
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: the maximal velocity of lactate oxidation is about 10% of pyruvate reduction
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Molinema dessetae
-
Substrates: pyruvate reduction is the favored reaction
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: involved in glycolysis
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, overview
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: mitochondrial metabolism of L-lactate plays a role in the response of potato to hypoxic stress
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: poor reaction
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + nicotinamide hypoxanthine dinucleotide
pyruvate + reduced nicotinamide hypoxanthine dinucleotide
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + nicotinamide hypoxanthine dinucleotide
pyruvate + reduced nicotinamide hypoxanthine dinucleotide
-
Substrates: -
Products: -
Products: -
r
2-oxobutanoate + NADH + H+
2-hydroxybutyrate + NAD+
-
Substrates: -
Products: -
Products: -
?
2-oxobutanoate + NADH + H+
2-hydroxybutyrate + NAD+
Sporolactobacillus inulinus YBS1-5
-
Substrates: -
Products: -
Products: -
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
Substrates: 107% of the activity with pyruvate
Products: -
Products: -
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
Substrates: 3% of the activity with pyruvate
Products: -
Products: -
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
Substrates: -
Products: -
Products: -
?
2-oxobutyrate + NADH
2-hydroxybutyrate + NAD+
-
Substrates: -
Products: -
Products: -
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: low activity
Products: -
Products: -
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: low activity
Products: -
Products: -
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: 11.5% of the activity with pyruvate
Products: -
Products: -
?
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
-
Substrates: 79.6% of the activity with pyruvate
Products: -
Products: -
?
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
Substrates: 14.6% of the activity with pyruvate
Products: -
Products: -
?
2-oxoglutarate + NADH + H+
2-hydroxyglutarate + NAD+
-
Substrates: -
Products: -
Products: -
?
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
-
Substrates: -
Products: -
Products: -
?
2-oxovalerate + NADH + H+
2-hydroxyvalerate + NAD+
Sporolactobacillus inulinus YBS1-5
-
Substrates: -
Products: -
Products: -
?
3-fluoropyruvate + NADH
?
-
Substrates: 33.6% of the activity with pyruvate
Products: -
Products: -
?
4-hydroxyphenylpyruvate + NADH + H+
L-4-hydroxyphenyllactate + NAD+
Substrates: -
Products: -
Products: -
?
4-hydroxyphenylpyruvate + NADH + H+
L-4-hydroxyphenyllactate + NAD+
Substrates: 11.1% of the activity with pyruvate
Products: -
Products: -
?
4-methyl-2-oxopentanoate + NADH
2-hydroxy-4-methylpentanoate + NAD+
-
Substrates: 39% of the activity with pyruvate
Products: -
Products: -
?
4-methyl-2-oxopentanoate + NADH
2-hydroxy-4-methylpentanoate + NAD+
-
Substrates: -
Products: -
Products: -
?
glyoxylate + NADH + H+
glycolate + NAD+
-
Substrates: best substrate of isoform LDHL1
Products: -
Products: -
?
glyoxylate + NADH + H+
glycolate + NAD+
Sporolactobacillus inulinus YBS1-5
-
Substrates: best substrate of isoform LDHL1
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
hydroxypyruvate + NADPH + H+
2,3-dihydroxypropanoate + NADP+
-
Substrates: -
Products: -
Products: -
?
L-lactate + NAD+
pyruvate + NADH
-
Substrates: the enzyme plays two important roles in heart metabolism, it catalyzes pyruvate reduction, mainly at the beginning of effort, or during hypoxia, and also catalyzes the oxidation of lactate released into the blood by other tissues, such as skeletal muscle, which would be used as substrate fuel by the heart mainly during steady-state exercise or during recuperation
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH
-
Substrates: LDH binds its substrate via the formation of a LDH/NADH-substrate encounter complex through a select-fit mechanism, whereby only a minority population of LDH/NADH is binding-competent, molecular dynamics calculations to explore the variations in structure accessible to the binary complex and binding-competent structures, active site interactions in the ternary complex, overview
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH
-
Substrates: the enzyme plays two important roles in heart metabolism, it catalyzes pyruvate reduction, mainly at the beginning of effort, or during hypoxia, and also catalyzes the oxidation of lactate released into the blood by other tissues, such as skeletal muscle, which would be used as substrate fuel by the heart mainly during steady-state exercise or during recuperation
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: no activity with D-lactate
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: no activity with D-lactate, activity of recombinant His6-tagged LctD is determined in the presence of the electron carriers 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide and phenazine methosulfate
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: no activity with D-lactate
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: no activity with D-lactate, activity of recombinant His6-tagged LctD is determined in the presence of the electron carriers 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl-2H-tetrazolium bromide and phenazine methosulfate
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: the wild-type V583 strain converts glucose almost exclusively to L-lactate under anaerobic conditions
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: amino acid residues involved in substrate and cofactor binding are Arg109, Asp168, Arg171, and His195
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: an encounter complex is formed between LDH-NAD+ and lactate, collapses to form a chemically active species and loop closure/opening steps
Products: -
Products: -
?
L-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
phenylpyruvate + NADH
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: 28% of the activity with pyruvate
Products: -
Products: -
?
phenylpyruvate + NADH
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: -
Products: -
Products: -
?
phenylpyruvate + NADH
phenyllactate + NAD+
-
Substrates: -
Products: -
Products: -
r
phenylpyruvate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: -
Products: -
Products: -
?
phenylpyruvate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
Sporolactobacillus inulinus YBS1-5
-
Substrates: -
Products: -
Products: -
?
phenylpyruvate + NADH + H+
L-phenyllactate + NAD+
Substrates: low activity
Products: -
Products: -
?
phenylpyruvate + NADH + H+
L-phenyllactate + NAD+
Substrates: low activity
Products: -
Products: -
?
phenylpyruvate + NADH + H+
L-phenyllactate + NAD+
Substrates: -
Products: -
Products: -
?
phenylpyruvate + NADH + H+
L-phenyllactate + NAD+
Substrates: 47.4% of the activity with pyruvate
Products: -
Products: -
?
pyruvate + NADH
L-lactate + NAD+
-
Substrates: lactate yield is increased in the pyruvate decarboxylase 1/alcohol dehydrogenase 1 double mutant compared with that in the single pyruvate decarboxylase 1 mutant
Products: -
Products: -
?
pyruvate + NADH
L-lactate + NAD+
Substrates: in the cell lysate of the host strain, L-LDH activity is hardly detectable during cultivation. As a consequence of transformation, the ratio between D- and L-isomers is changed due to the increment of L-lactate and the decrement of D-lactate, but there are no significant differences in total lactate concentration between the host and transformant cells. In the transformant harboring pLC18lld, L-LDH activity is detected during the entire cultivation period. L-LDH activity increases rapidly to the maximum level (0.18 U/mg protein) between the early- and mid-exponential growth phases (0-8 h), and decreases thereafter during the stationary phase
Products: -
Products: -
?
pyruvate + NADH
L-lactate + NAD+
Substrates: LDH1 has an important physiological function, in addition to being a glycolytic enzyme and differentiation marker. The enzymatic activity, growth, and virulence of tachyzoites are unaffected by the presence of the recombinant protein. Overexpression of LDH1 enhances the parasite's ability to differentiate
Products: -
Products: -
?
pyruvate + NADH
L-lactate + NAD+
Substrates: LDH2 has an important physiological function, in addition to being a glycolytic enzyme and differentiation marker. The enzymatic activity, growth, and virulence of tachyzoites are unaffected by the presence of the recombinant protein. Overexpression of LDH2 enhances the parasite's ability to differentiate
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: active site structure and substrate binding, overview
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: active site structure and substrate binding, overview
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: study of the dependence of the chemical reaction mechanism of lactate dehydrogenase on the protonation state of titratable residues and on the level of the quantum mechanical description by means of hybrid quantum-mechanical methods
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: the maximal velocity of lactate oxidation is only 10% of pyruvate reduction
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: inactivation of the lshL does not abolish the production of L-lactate, but the lactate final concentration decreases about 25% compared to the wild-type, suggesting the presence of at least a second L-Ldh
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Lactobacillus mesenteroides
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: the maximal velocity of lactate oxidation is only 10% of pyruvate reduction
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Molinema dessetae
-
Substrates: pyruvate reduction is the favored reaction
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: LdhB enzymes from type-I isolate NRRL 395 and type-II isolate 99-880 show reductive LDH activity, but no oxidative LDH activity, overview
Products: -
Products: -
ir
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: the nitric oxide-inducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity, L-lactate production allows Staphylococcus aureus to maintain redox homeostasis during nitrosative stress and is essential for virulence, regulation, overview
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
ir
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: D-glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase have a functional interaction that can affect NAD+/NADH metabolism and glycolysis in living cells
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: active site structure and substrate binding, overview
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: terminal enzyme in aerobic glycolysis necessary for NAD+ regeneration
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: enzyme activity increases in response to infection by black-rot fungus but decreases in response to cutting
Products: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: key enzyme in anaerobic metabolism which converts pyruvate to lactate
Products: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
Sporolactobacillus inulinus YBS1-5
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: an encounter complex is formed between LDH-NADH and pyruvate, collapses to form a chemically active species and loop closure/opening steps
Products: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: last step in anaerobic glycolysis
Products: -
Products: -
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
-
Substrates: 15% of the activity with NADH
Products: -
Products: -
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
-
Substrates: 20% of the activity with NADH
Products: -
Products: -
?
pyruvate + NADPH + H+
(S)-lactate + NADP+
-
Substrates: 34% of the activity with NADH
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
Substrates: amino acid sequence, structure and kinetic comparison of L-LDH with citrate synthase, EC 2.3.3.1, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: amino acid sequence, structure and kinetic comparison of L-LDH with citrate synthase, EC 2.3.3.1, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: in addition of lactate dehydrogenase activity, the epsilon-crystallin also possesses the enzymatic activity of malate dehydrogenase
Products: -
Products: -
?
additional information
?
-
-
Substrates: Bacillus subtilis fermentation pathways, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also utilizes NADP(H)
Products: -
Products: -
?
additional information
?
-
-
Substrates: Bacillus subtilis fermentation pathways, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also utilizes NADP(H)
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate binding structure, overview. The side chain of the Arg171 residue of LDH-2 seems to be important for the binding of pyruvate, pointing toward the pyruvate-binding site
Products: -
Products: -
?
additional information
?
-
Substrates: substrate binding structure, overview. The side chain of the Arg171 residue of LDH-2 seems to be important for the binding of pyruvate, pointing toward the pyruvate-binding site
Products: -
Products: -
?
additional information
?
-
Substrates: substrate binding structure, overview. The side chain of the Arg171 residue of LDH-2 seems to be important for the binding of pyruvate, pointing toward the pyruvate-binding site
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate binding structure, overview. The side chain of the Arg171 residue of LDH-2 seems to be important for the binding of pyruvate, pointing toward the pyruvate-binding site
Products: -
Products: -
?
additional information
?
-
Substrates: substrate analogue oxamate is isoelectric and isosteric to pyruvate and has binding kinetics very similar to that of pyruvate. As the substrate approaches the catalytic site, a catalytically key surface loop (residues 98-110) closes over the ligand, bringing residue Arg109 into hydrogen bonding contact with ligand, water leaves the pocket, and the pocket geometry rearranges to allow for favorable interactions between the cofactor and the ligand, which facilitates on-enzyme catalysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate analogue oxamate is isoelectric and isosteric to pyruvate and has binding kinetics very similar to that of pyruvate. As the substrate approaches the catalytic site, a catalytically key surface loop (residues 98-110) closes over the ligand, bringing residue Arg109 into hydrogen bonding contact with ligand, water leaves the pocket, and the pocket geometry rearranges to allow for favorable interactions between the cofactor and the ligand, which facilitates on-enzyme catalysis
Products: -
Products: -
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additional information
?
-
Substrates: L-nLDH shows higher specificity towards pyruvate esters, such as methyl pyruvate and ethyl pyruvate. Very poor activity with 4-methyl-2-oxovalerate
Products: -
Products: -
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additional information
?
-
Substrates: L-nLDH shows higher specificity towards pyruvate esters, such as methyl pyruvate and ethyl pyruvate. Very poor activity with 4-methyl-2-oxovalerate
Products: -
Products: -
?
additional information
?
-
-
Substrates: LDH is essential for continuous glycolysis necessary for accelerated tumor growth and increased LDH activity occurs already in grade 1 EC carcinomas
Products: -
Products: -
?
additional information
?
-
Substrates: amino acid sequence, structure and kinetic comparison of L-LDH with citrate synthase, EC 2.3.3.1, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: amino acid sequence, structure and kinetic comparison of L-LDH with citrate synthase, EC 2.3.3.1, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is unlikely to catalyze lactate oxidation at an appreciable rate under physiological conditions
Products: -
Products: -
?
additional information
?
-
Substrates: intracellular isozyme regulation in relation to pH, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: intracellular isozyme regulation in relation to pH, overview
Products: -
Products: -
?
additional information
?
-
Substrates: intracellular isozyme regulation in relation to pH, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the system regulating the cellular pH and/or controlling the concentration of reducing equivalents in the cytoplasm of leaf cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: LDH is critically implicated in tumor growth
Products: -
Products: -
?
additional information
?
-
-
Substrates: LDH is critically implicated in tumor growth
Products: -
Products: -
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additional information
?
-
-
Substrates: the formation of lactate in satellite gliocytes is induced by nicotinic cholinergic synapses directly involved in neuron-glial interactions and in controlling the activity of the LDH enzyme system in sympathetic neurons
Products: -
Products: -
?
additional information
?
-
-
Substrates: L-lactate dehydrogenase catalyzes the conversion of pyruvate to L-lactate using NADH as a cofactor
Products: -
Products: -
?
additional information
?
-
-
Substrates: Plasmodium falciparum lactate dehydrogenase has L-malate dehydrogenase activity, which plays a role in the tricarboxylic acid cycle
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: exogenous L-lactate enters mitochondria by a proton-compensated process, is converted to pyruvate, which is exported to the cytoplasm via a non-energy-competent L-lactate-pyruvate shuttle, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
Streptococcus mitior
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: fructose 1,6-diphosphate activated enzymes are virtually nonreversible, enzymes which do not require fructose 1,6-diphosphate catalyze reversible reactions
Products: -
Products: -
?
additional information
?
-
-
Substrates: the heart-type isozyme interacts with liposomes made of acidic phospholipids, such as phosphatidylserine or cardiolipin, most effectively at low pH close to the isoelectric point of the isozyme of pH 5.5 strongly involving the enzyme's NADH-cofactor binding site, no interaction with liposomes of the muscle-type isozyme, overview
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Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD(P)+
pyruvate + NAD(P)H + H+
-
Substrates: L-lactate transport and metabolism, regulation and localization of enzyme participating in the pathway, overview
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: the astrocytic cell line CCF-STTG1 is able to consume lactate to generate ATP via oxidative phosphorylation, overview
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: since the mitochondrial metabolism of (S)-lactate results in synthesis and export of oxaloacetate, malate and citrate into the extramitochondrial phase, an anaplerotic role for the mitochondrial (S)-lactate metabolism is proposed
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
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r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Lactococcus cremoris MG1363
-
Substrates: lactate oxidation does not occur unless pyruvate and especially NADH drop to low levels
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis
Products: -
Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: LDH is a key enzyme in homolactic fermentation catalyzing the reduction of pyruvate to lactate with the concomitant oxidation of NADH, LDH and LDHB are involved in glycolysis
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Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: -
Products: -
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r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: involved in glycolysis
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r
(S)-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: mitochondrial metabolism of L-lactate plays a role in the response of potato to hypoxic stress
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Products: -
r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
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r
(S)-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-lactate + NAD+
pyruvate + NADH
-
Substrates: the enzyme plays two important roles in heart metabolism, it catalyzes pyruvate reduction, mainly at the beginning of effort, or during hypoxia, and also catalyzes the oxidation of lactate released into the blood by other tissues, such as skeletal muscle, which would be used as substrate fuel by the heart mainly during steady-state exercise or during recuperation
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r
L-lactate + NAD+
pyruvate + NADH
-
Substrates: the enzyme plays two important roles in heart metabolism, it catalyzes pyruvate reduction, mainly at the beginning of effort, or during hypoxia, and also catalyzes the oxidation of lactate released into the blood by other tissues, such as skeletal muscle, which would be used as substrate fuel by the heart mainly during steady-state exercise or during recuperation
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r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: no activity with D-lactate
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r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: no activity with D-lactate
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r
L-lactate + NAD+
pyruvate + NADH + H+
-
Substrates: the wild-type V583 strain converts glucose almost exclusively to L-lactate under anaerobic conditions
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r
L-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
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r
L-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
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r
L-lactate + NAD+
pyruvate + NADH + H+
Substrates: -
Products: -
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r
phenylpyruvate + NADH
phenyllactate + NAD+
-
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
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r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
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r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
Products: -
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r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
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r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: inactivation of the lshL does not abolish the production of L-lactate, but the lactate final concentration decreases about 25% compared to the wild-type, suggesting the presence of at least a second L-Ldh
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: LdhB enzymes from type-I isolate NRRL 395 and type-II isolate 99-880 show reductive LDH activity, but no oxidative LDH activity, overview
Products: -
Products: -
ir
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: the nitric oxide-inducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity, L-lactate production allows Staphylococcus aureus to maintain redox homeostasis during nitrosative stress and is essential for virulence, regulation, overview
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: -
Products: -
Products: -
r
pyruvate + NADH + H+
(S)-lactate + NAD+
-
Substrates: D-glyceraldehyde-3-phosphate dehydrogenase and L-lactate dehydrogenase have a functional interaction that can affect NAD+/NADH metabolism and glycolysis in living cells
Products: -
Products: -
?
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: LDH catalyzes the conversion of pyruvate to lactate with concomitant oxidation of NADH during the last step in anaerobic glycolysis
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r
pyruvate + NADH + H+
(S)-lactate + NAD+
Substrates: terminal enzyme in aerobic glycolysis necessary for NAD+ regeneration
Products: -
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?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: enzyme activity increases in response to infection by black-rot fungus but decreases in response to cutting
Products: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: key enzyme in anaerobic metabolism which converts pyruvate to lactate
Products: -
Products: -
?
pyruvate + NADH + H+
L-lactate + NAD+
-
Substrates: last step in anaerobic glycolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: Bacillus subtilis fermentation pathways, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: Bacillus subtilis fermentation pathways, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: LDH is essential for continuous glycolysis necessary for accelerated tumor growth and increased LDH activity occurs already in grade 1 EC carcinomas
Products: -
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?
additional information
?
-
-
Substrates: the enzyme is unlikely to catalyze lactate oxidation at an appreciable rate under physiological conditions
Products: -
Products: -
?
additional information
?
-
Substrates: intracellular isozyme regulation in relation to pH, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: intracellular isozyme regulation in relation to pH, overview
Products: -
Products: -
?
additional information
?
-
Substrates: intracellular isozyme regulation in relation to pH, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is a component of the system regulating the cellular pH and/or controlling the concentration of reducing equivalents in the cytoplasm of leaf cells
Products: -
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?
additional information
?
-
-
Substrates: LDH is critically implicated in tumor growth
Products: -
Products: -
?
additional information
?
-
-
Substrates: LDH is critically implicated in tumor growth
Products: -
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?
additional information
?
-
-
Substrates: L-lactate dehydrogenase catalyzes the conversion of pyruvate to L-lactate using NADH as a cofactor
Products: -
Products: -
?
additional information
?
-
-
Substrates: exogenous L-lactate enters mitochondria by a proton-compensated process, is converted to pyruvate, which is exported to the cytoplasm via a non-energy-competent L-lactate-pyruvate shuttle, overview
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-acetyl-pyridine adenine dinucleotide
i.e. APAD+, 3-acetylpyridine adenine dinucleotide, analogue of NAD+
3-acetylpyridine adenine dinucleotide
-
wild-type and S163 L mutant protein bind 3-acetylpyridine adenine dinucleotide more tightly than they bind NADH
3-acetylpyridine adenine dinucleotide
-
assay is based on reduction of 3-acetyl pyridine adenine dinucleotide that is specific for PfLDH, which allows the distinction of PfLDH from that of the host erythrocyte
NAD+
wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+
NAD+
-
the coenzyme is in an open conformation and the adenine ribose ring of it is surrounded by Asp 38, Val 39, and Gly 99. Asp 38 and Gly 99 give some specificity to the adenine orientation, overview
NADH
-
the coenzyme is in an open conformation and the adenine ribose ring of it is surrounded by Asp 38, Val 39, and Gly 99. Asp 38 and Gly 99 give some specificity to the adenine orientation, Asp 38 is an important residue in stabilizing NADH binding, overview
NADH
NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH did not change with pH
NADH
-
the NADH-cofactor binding site of heart LDH is involved in the interaction of the isozyme with liposomes made of acidic phospholipids, overview
NADH
kinetic modelling of NADH binding to the enzyme, overview
NADP+
wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+
additional information
-
the enzyme also utilizes both NAD(H) and NADP(H)
-
additional information
Cryptosporidium parvum lactate dehydrogenase prefers the acetylpyridine analogue of NADH as a cofactor. NADH/APADH and substrate binding site structures, overview. replacement of the conserved serine residue by Met163 in CpLDH allows a better packing environment for the acetyl of APAD+
-
additional information
-
Cryptosporidium parvum lactate dehydrogenase prefers the acetylpyridine analogue of NADH as a cofactor. NADH/APADH and substrate binding site structures, overview. replacement of the conserved serine residue by Met163 in CpLDH allows a better packing environment for the acetyl of APAD+
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cd2+
Co2+
Mg2+
Mn2+
Zn2+
additional information
Ca2+
-
50% of the stimulation with Mn2+, Co2+ or Cd2+, higher concentrations required
Co2+
-
activation involves association of enzyme dimers, followed by ligand binding
additional information
Ca2+, Ba2+, and Mg2+ ions are as effective as Mn2+ at pH 6.5 in enzyme activation
additional information
not or poorly affected by 1 mM of EDTA, ATP, Mg2+, Co2+, Ca2+, Mn2+, and Ni2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
1-hydroxy-6-phenyl-4-(trifluoromethyl)-1H-indol-2-carboxylic acid
a N-hydroxyindole, NH1-1, and a competitive inhibitor with respect to both NADH and pyruvate
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
3-((3-carbamoyl-7-(3,5-dimethylisoxazol-4-yl)-6-methoxyquinolin-4-yl) amino) benzoic acid
a quinoline-3-sulfonamide, competitive inhibitor with respect to both NADH and pyruvate
3-([3-carbamoyldimethoxypyrimidin-7-(2,4-dimethoxypyrimidin-5-yl)quinolin-4-yl]amino)benzoic acid
enzyme binding structure, overview
3-acetylpyridine adenine dinucleotide
-
the enzyme exhibits characteristic reduced substrate inhibition and enhanced kcat
3-Aminopyridine adenine dinucleotide
-
competitive versus NAD+ and noncompetitive versus L-lactate
3-[7-(2,4-dimethoxypyrimidin-5-yl)-3-sulfamoylquinolin-4-yl]aminobenzoic acid
enzyme binding structure, overview
6-benzyl-3,4-dihydroxy-7-methyl-1-propylnaphthalene-2-carboxylic acid
FX11, a competitive inhibitor with respect to both NADH and pyruvate
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl acetate
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl butanoate
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl pentanoate
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl propanoate
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
ascorbate
-
at concentrations normally found in tissue. It is proposed that ascorbate facilitates the storage of glycogen in muscle at rest by inhibiting glycolysis. Aldolase and muscle G-actin protect and reverse inhibition
AZ-33
a malonic derivative, a competitive inhibitor with respect to both NADH and pyruvate
cardiolipin
-
IC50: 0.00005 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
Chinese gall
ethanol extract of the Chinese gall, commonly named Wu Bei Zi, strongly inhibits the enzyme
-
Cu[Ac]2[2,2'-bipyridine]
-
analysis of interaction with the LDH isozymes and their modulation, significantly inhibits LDH in liver, kidney, heart, spleen, brain and skeletal muscle tissues, overview
dicholesteroyl diselenide
-
inhibition of different isoforms of lactate dehydrogenase by dicholesteroyl diselenide possibly involves the modification of the thiol groups at the NAD+ binding site of the enzyme. Exerts profound concentration dependent inhibitory effect on the activity of renal LDH. Inhibitory effect on hepatic LDH is markedly pronounced at 2, 4, 8 and 10 microM. Strongly inhibits cardiac LDH activity when NAD+ is omitted from the pre-incubating medium than when lactate is absent from the pre-incubating medium, significantly inhibits the enzyme activity at 1, 2, 4, and 8 microM
diphenyl diselenide
-
inhibition of different isoforms of lactate dehydrogenase by diphenyl diselenide possibly involves the modification of the thiol groups at the NAD+ binding site of the enzyme. Inhibitory effect on hepatic LDH is markedly different at 10 microM. Markedly inhibits cardiac LDH activity at 8 and 10 microM
epigallocatechin
the most potent compound with anti-LDH-5 activity under both normoxia and hypoxia conditions
galloflavin
a blocker of LDH-5-ssDNA interactions, preventing RNA synthesis
Lactate
-
a high concentration of lactate has a weak inhibitory effect on the pyruvate reduction reaction activity but is meaningful for a significant lactate oxidation rate as the K m value of LDHA for L-lactate is very high
methyl 1-hydroxy-6-phenyl-4-(trifluoromethyl)-1H-indol-2-carboxylate
a N-hydroxyindole, NH1-2, and a competitive inhibitor with respect to both NADH and pyruvate
nicotinic acid adenine dinucleotide
-
competitive versus NAD+ and noncompetitive versus L-lactate
o-phthalaldehyde
-
modification not only results in inactivation of the enzyme, but also leads to the enzymes dissociation and partial unfolding
phosphatidylserine
-
IC50: 0.0013 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
Spatholobus suberectus extract
the extract has a strong inhibitory effect on LDH-5 expression and activity inboth estrogen-dependent and estrogen-independent human breast cancer cells
-
Thionicotinamide adenine dinucleotide
-
competitive versus NAD+ and noncompetitive versus L-lactate
Urea
-
enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, LDH is more sensitive than MDH, overview
Zn[Ac]2[2,2'-bipyridine]
-
analysis of interaction with the LDH isozymes and their modulation, significantly inhibits LDH in liver, kidney, and heart, but not in spleen, brain and skeletal muscle tissues, overview
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
-
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
-
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
-
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
-
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
-
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
-
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
-
-
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
-
-
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
-
-
2,3-dihydroxy-6,7-dimethyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(2-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(2-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(3-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(3-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(4-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
2,3-dihydroxy-6-methyl-7-(4-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid
-
trophozoites are the most susceptible stages to exposure to 4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid
7-(4-chlorobenzyl)-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
7-(4-chlorobenzyl)-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
7-benzyl-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
7-benzyl-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
-
7-benzyl-2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
-
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
-
-
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl acetate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl acetate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl butanoate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl butanoate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl pentanoate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl pentanoate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl propanoate
-
-
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl propanoate
-
-
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
-
-
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
-
-
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
-
-
ADP
-
ADP is a more severe inhibitor and has a more severe inhibitory effect on the lactate oxidation reaction. But its relative inhibition on reverse reactions is weak at low ADP concentrations
ATP
-
inhibitory effects of ATP on both directions are weak and similar as both rates remain above 80% in the presence of 8 mM ATP
ATP
-
at neutral or alkaline pH ATP behaves as a weak competitive inhibitor, potent inhibitor at acid pH values
D-fructose 1,6-bisphosphate
-
slightly inhibits activity of hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
D-fructose 1,6-bisphosphate
-
slightly inhibits activity of hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
fructose 1,6-bisphosphate
-
10 mM significantly inhibits LDHB by 23% in a non-competitive manner. Level of inhibition seems to be even more pronounced at pH 6.2, compared to the optimal pH 6.8. At the more acidic pH and in the presence of 10 mM, LDHB shows a 42% decrease in activity
fructose 1,6-bisphosphate
-
10 mM significantly inhibits LDHA abd LDHB (by 86%) in a non-competitive manner. Level of inhibition seems to be even more pronounced at pH 6.2, compared to the optimal pH 6.8. At the more acidic pH and in the presence of 10 mM, there is almost a 97% decrease in activity for LDHB
fructose 1,6-diphosphate
-
activation at low concentrations, inhibition at high concentrations
gossypol
-
a polyphenolic binaphthyl disesquiterpene from Gossypium sp.
methylmalonate
-
IC50: 4.6 mM (enzyme from brain), 4.6 mM (enzyme from liver)
NAD+
-
substrate inhibition due to an abortive NAD+-pyruvate complex reducing the steady state concentration of functional LDH
oxamate
an inhibitor of gluconeogenesis, which suppresses cell proliferation through induction of G2/M or G0/G1 cell cycle arrest and promotion of apoptosis
phosphate
-
slight activation of non-activated enzyme, inhibition of fructose 1,6-diphosphate activated enzyme
pyruvate
-
substrate inhibition due to an abortive NAD+-pyruvate complex reducing the steady state concentration of functional LDH
pyruvate
-
substrate inhibition by pyruvate is related to the formation of an enzyme-pyruvate-NAD+complex
pyruvate
-
substrate inhibition in wild type enzyme, lower substrate inhibition in mutant S163L
pyruvate
-
the enzyme shows substrate inhibition, inhibition mechanism, overview
pyruvate
-
strong substrate inhibition at high concentrations, fructose 1,6-diphosphate activated enzyme
additional information
-
the Aggregatibacter actinomycetemcomitans L-lactate dehydrogenase, unlike homologous enzymes, is not feedback inhibited by pyruvate, pyruvate is a poor inhibitor of L-lactate dehydrogenase activity
-
additional information
-
loss of LDH activity with increasing pressure and time treatment due to the combined effects of denaturation and aggregation, overview
-
additional information
CpLDH does not display any measurable inhibition to pyruvate concentrations up to at least 20 mM in contrast to many other LDHs
-
additional information
-
CpLDH does not display any measurable inhibition to pyruvate concentrations up to at least 20 mM in contrast to many other LDHs
-
additional information
-
blockade of nicotinic cholinoreceptors significantly decreases total LDH activity and H- and M-isoform activities in neurons. LDH activity decreases by 41.5% and 71% in conditions of partial and complete blockade, respectively. Decreases in H-isoform activity are by 25% in partial blockade and 42% in complete blockade and decreases in M-isoform activity are by 35% and 62%. In partial and complete blockade, the activity of LDH and its H- and M-isoforms decrease significantly in proportion to the number of blocked nicotinic cholinoreceptors. In satellite gliocytes, increases in the extent of blockade are associated with decreases in the activity only of the M-isoform (by 43% in partial blockade and 55.5% in complete blockade), while the activity of the H-isoform does not change. In partial blockade, the LDH isoenzyme profile of satellite gliocytes shifts towards the neuronal isoform, while in complete blockade there is no difference from the LDH isoenzyme profile of intact neurons
-
additional information
-
inhibition mechanism, the plasmodial enzyme possesses a five-residue insertion in the substrate-specificity loop and exhibits less marked substrate inhibition than its mammalian counterparts, overview
-
additional information
-
short-term storage in Krebs-Henseleit buffer for 24 h at 4°C does not affect LDH activity, but a 42% decline occurs at 23°C. After 48 h, activity declines 11% at 4°C and 98% at 23°C. Frozen storage results in a 40% loss at -80°C and a 79% loss at -20°C
-
additional information
-
NADH, NAD+, ATP, ADP, AMP, and pyruvate inhibit the interaction of the heart-type isozyme with acidic phospholipid liposomes, potency in descending order. NADP+, GTP, CTP, UTP and lactate are ineffective, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-fructose 1,6-diphosphate
activates wild-type enzyme and mutant enzymes F16Q/I37K/D38SC81S/N85R and F16Q/C81S/N85R
fructose 1,6-bisphosphate
assures that the protein forms tetrameric uniformity and serves as an allosteric activator of the enzyme
phosphate
-
slight activation of not activated enzyme, inhibition of fructose 1,6-diphosphate activated enzyme
D-fructose 1,6-bisphosphate
-
activates the pyruvate reduction
D-fructose 1,6-bisphosphate
activation constants of isozymes at different pH values, overview
D-fructose-1,6-bisphosphate
the allosteric enzyme requires fructose-1,6-bisphosphate (FBP), an intermediate in the glycolysis pathway, for catalytic activities. FBP may play a role in stabilizing and maintaining the tetrameric structure
D-fructose-1,6-bisphosphate
enzyme binding structure, overview. The allosteric enzyme requires fructose-1,6-bisphosphate (FBP), an intermediate in the glycolysis pathway, for catalytic activities. FBP may play a role in stabilizing and maintaining the tetrameric structure
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
binding of fructose 1,6-diphosphate induces a conformational change in the enzyme which leads to increased activity, without association of enzyme subunits or dimers
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
Lactobacillus mesenteroides
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
binding of fructose 1,6-diphosphate induces a conformational change in the enzyme, producing a form with reduced protein fluorescence and increased activity towards pyruvate reduction
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
concentration required for 50% maximal activity is about 0.15 mM
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
Streptococcus mitior
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
at pH 7.5 lactate dehydrogenase activity is absent without fructose 1,6-diphosphate, from pH 5.0 to pH 7.0 lactate dehydrogenase is present without fructose 1,6-diphosphate but is greater in the presence of the activator
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
maximal activation is about: 0.03 mM at pH 6.0, 0.2 mM at pH 7.1, 2 mM at pH 8.0 and 7 mM at pH 9.0
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
fructose 1,6-diphosphate
-
L-lactate dehydrogenase form which is not activated by fructose 1,6-diphosphate
additional information
thermodynamic activation parameters, overview
-
additional information
-
thermodynamic activation parameters, overview
-
additional information
thermodynamic activation parameters, overview
-
additional information
-
thermodynamic activation parameters, overview
-
additional information
the enzyme also shows some activity in the absence of D-fructose-1,6-bisphosphate, with a pH optimum of pH 4.0
-
additional information
direct phosphorylation of LDHA at Y10 and Y83 strongly enhances LDH-5 tetramer formation and cofactor binding, resulting in significantly increased LDH enzymatic activity
-
additional information
-
hearts perfused with Krebs-Henseleit buffer, subjected to 30 min of global ischemia followed by normoxic reperfusion, which causes tissue damage and elevate LDH release
-
additional information
-
presence of an amino terminal fusion with a small ubiquitin-related modifier, SUMO, increases the oxidative activity per micromol protein by more than 100fold, while having little effect on the reductive LDH activity
-
additional information
-
presence of an amino terminal fusion with a small ubiquitin-related modifier, SUMO, increases the oxidative activity per micromol protein by more than 100fold, while having little effect on the reductive LDH activity
-
additional information
thermodynamic activation parameters, overview
-
additional information
-
thermodynamic activation parameters, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.7
NADP+
25°C, pH 8, mutant enzyme F16Q/I37K/D38SC81S/N85R, activated by fructose 1,6-diphosphate
10.73
(S)-lactate
pH 8.0, temperature not specified in the publication, healthy breast tissue enzyme
21.78
(S)-lactate
pH 8.0, temperature not specified in the publication, breast cancer tissue enzyme
158
(S)-lactate
-
pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate
0.152
L-lactate
-
pH not specified in the publication, temperature not specified in the publication
0.0081
NAD+
25°C, pH 8, mutant enzyme F16Q/C81S/N85R, activated by fructose 1,6-diphosphate
0.105
NAD+
25°C, pH 8, wild-type enzyme, activated by fructose 1,6-diphosphate
0.38
NAD+
-
pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate
0.5
NAD+
pH 8.0, temperature not specified in the publication, healthy breast tissue enzyme
0.99
NAD+
pH 8.0, temperature not specified in the publication, breast cancer tissue enzyme
0.05
NADH
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
0.066
NADH
-
pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate
0.08
NADH
-
pH 6.9, 90 mM Tris-maleate buffer, pH 6.9, 0.5 mM fructose 1,6-diphosphate
0.08
NADH
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
0.11
NADH
pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
0.15
NADH
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
0.18
NADH
pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
0.19
NADH
-
measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
0.19
NADH
-
measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
0.2
NADH
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
0.26
NADH
pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
0.41
NADH
pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
0.9
NADH
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate
0.93
NADH
pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
1.86
phenylpyruvate
mutant Q88R, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
2.5 - 5
phenylpyruvate
mutant I229A, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
3.5
phenylpyruvate
wild-type, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
0.06
pyruvate
pH 6.0, 25°C, recombinant wild-type enzyme
0.2
pyruvate
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
0.8
pyruvate
-
measured with D-fructose 1,6-bisphosphate, wild-type enzyme
0.93
pyruvate
pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
1.5
pyruvate
-
pH 6.9, 90 mM Tris-maleate buffer, pH 6.9, 0.5 mM fructose 1,6-diphosphate
1.95
pyruvate
-
pH 7.0, 30°C, recombinant enzyme, with 1 mM D-fructose-1,6-bisphophate
2.2
pyruvate
pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
2.3
pyruvate
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
2.7
pyruvate
pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
2.76
pyruvate
-
pH 6.0, 25°C, recombinant wild-type enzyme in presence of fructose 1,6-bisphosphate
3
pyruvate
pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
3.7
pyruvate
-
pH 6.0, 25°C, recombinant mutant D38R in presence of fructose 1,6-bisphosphate
3.8
pyruvate
pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
6.8
pyruvate
-
measured with D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
6.8
pyruvate
-
measured with D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
7
pyruvate
-
measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
7
pyruvate
-
measured without D-fructose 1,6-bisphosphate, hybrid enzyme constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331)
13
pyruvate
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
15
pyruvate
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate
19.3
pyruvate
-
pH 6.0, 25°C, recombinant mutant D38R in absence of fructose 1,6-bisphosphate
32
pyruvate
-
pH 6.0, 25°C, recombinant wild-type enzyme in absence of fructose 1,6-bisphosphate
34
pyruvate
-
measured without D-fructose 1,6-bisphosphate, wild-type enzyme
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values at position of temperatur minimum
-
additional information
additional information
-
KM-values for mutant enzymes with enlarged loop
-
additional information
additional information
-
steady-state and transient kinetics, rapid kinetics of the multiple-turnover reaction, overview
-
additional information
additional information
an allosteric enzyme
-
additional information
additional information
-
an allosteric enzyme
-
additional information
additional information
isozymes LDH and LDHB, kinetic analysis, NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH does not change with pH
-
additional information
additional information
-
isozymes LDH and LDHB, kinetic analysis, NADH saturation curves of LDHB become more sigmoidal with increasing pH from pH 5.5 to pH 7.2, resulting in a marked decrease of the affinity for this cofactor, while the Km of LDH for NADH does not change with pH
-
additional information
additional information
-
stopped-flow kinetics, steady-state kinetics, and thermodynamics of free and NADH-bound enzyme, overview
-
additional information
additional information
kinetics, the enzyme is allosteric in presence of D-fructose 1,6-bisphosphate, overview
-
additional information
additional information
-
alternative allosteric regulation mechanism of an acidophilic L-lactate dehydrogenase, kinetic analysis of the recombinant enzyme, overview
-
additional information
additional information
alternative allosteric regulation mechanism of an acidophilic L-lactate dehydrogenase, kinetic analysis of the recombinant enzyme, overview
-
additional information
additional information
-
enzyme kinetics, ordered bibi kinetic mechanism of nLDH with the coenzyme binding first
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
LDH has different kinetic characteristics in breast tumors compared to normal breast tissues. Tumor LDH affinity in the pyruvate reduction reaction is the same as for normal LDH but Vmax of cancerous LDH is higher relative to normal LDH. In the lactate oxidation reaction, affinity of tumor LDH for lactate and NAD+ is lower than for normal LDH, also the enzyme efficiency for lactate and NAD+ is higher in normal samples. The activation energy for the pyruvate reduction reaction is higher in cancerous tissues. The enzyme in forward reaction in both tissues displays sigmoidal kinetics with respect to pyruvate and NADH
-
additional information
additional information
-
LDH has different kinetic characteristics in breast tumors compared to normal breast tissues. Tumor LDH affinity in the pyruvate reduction reaction is the same as for normal LDH but Vmax of cancerous LDH is higher relative to normal LDH. In the lactate oxidation reaction, affinity of tumor LDH for lactate and NAD+ is lower than for normal LDH, also the enzyme efficiency for lactate and NAD+ is higher in normal samples. The activation energy for the pyruvate reduction reaction is higher in cancerous tissues. The enzyme in forward reaction in both tissues displays sigmoidal kinetics with respect to pyruvate and NADH
-
additional information
additional information
Michaelis-Menten and Hanes-Woolf kinetic analysis and thermodynamics of isozymes H4, M4, and H2M2, overview. The Km values for heteroterameric H2M2-mediated catalysis of pyruvate or lactate are between those for the homotetrameric isozymes, M4 and H4, whereas the Vmax values are similar. The Km and Vmax values for H2M2-mediated catalysis of NADH are not significantly different among LDH isozymes. The values for activation energy and van't Hoff enthalpy changes for pyruvate reduction of H2M2 are between those for the homotetrameric isozymes. The temperature for half residual activity of H2M2 is closer to that for M4 than for H4
-
additional information
additional information
Michaelis-Menten and Hanes-Woolf kinetic analysis and thermodynamics of isozymes H4, M4, and H2M2, overview. The Km values for heteroterameric H2M2-mediated catalysis of pyruvate or lactate are between those for the homotetrameric isozymes, M4 and H4, whereas the Vmax values are similar. The Km and Vmax values for H2M2-mediated catalysis of NADH are not significantly different among LDH isozymes. The values for activation energy and van't Hoff enthalpy changes for pyruvate reduction of H2M2 are between those for the homotetrameric isozymes. The temperature for half residual activity of H2M2 is closer to that for M4 than for H4
-
additional information
additional information
-
Michaelis-Menten and Hanes-Woolf kinetic analysis and thermodynamics of isozymes H4, M4, and H2M2, overview. The Km values for heteroterameric H2M2-mediated catalysis of pyruvate or lactate are between those for the homotetrameric isozymes, M4 and H4, whereas the Vmax values are similar. The Km and Vmax values for H2M2-mediated catalysis of NADH are not significantly different among LDH isozymes. The values for activation energy and van't Hoff enthalpy changes for pyruvate reduction of H2M2 are between those for the homotetrameric isozymes. The temperature for half residual activity of H2M2 is closer to that for M4 than for H4
-
additional information
additional information
Michaelis-Menten kinetic modelling, detailed overview. NADH can bind only to the open-loop apoenzyme, substrate analogue oxamate can bind only to the bsLDH·NADH binary complex in the open-loop conformation, and oxamate binding is followed by closing of the active site loop preventing oxamate unbinding. The open and closed states of the loop are in dynamic equilibrium and interconvert on the submillisecond time scale. This interconversion strongly accelerates with an increase in temperature because of significant enthalpy barriers. Binding of NADH to bsLDH results in minor changes of the loop dynamics and does not shift the open-closed equilibrium, but binding of the oxamate substrate mimic shifts this equilibrium to the closed state. At high excess oxamate concentrations where all active sites are nearly saturated with the substrate mimic, all active site mobile loops are mainly closed, kinetic analysis, overview
-
additional information
additional information
-
Michaelis-Menten kinetic modelling, detailed overview. NADH can bind only to the open-loop apoenzyme, substrate analogue oxamate can bind only to the bsLDH·NADH binary complex in the open-loop conformation, and oxamate binding is followed by closing of the active site loop preventing oxamate unbinding. The open and closed states of the loop are in dynamic equilibrium and interconvert on the submillisecond time scale. This interconversion strongly accelerates with an increase in temperature because of significant enthalpy barriers. Binding of NADH to bsLDH results in minor changes of the loop dynamics and does not shift the open-closed equilibrium, but binding of the oxamate substrate mimic shifts this equilibrium to the closed state. At high excess oxamate concentrations where all active sites are nearly saturated with the substrate mimic, all active site mobile loops are mainly closed, kinetic analysis, overview
-
additional information
additional information
-
Vmax in the pyruvate-reducing direction is significantly higher for the enzyme from anoxic crayfish whereas in the lactate-oxidizing direction the Vmax is significantly higher for the aerobic control enzyme
-
additional information
additional information
-
Km values for pyruvate, NADH, (S)-lactate and NAD+ are measured in the solubilized mirochondrial Hep G2 fractions. They differ from the values measured in the cytosolic fractions
-
additional information
pyruvate
-
the enzyme shows hyperbolic dependence on the substrate concentration
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
23
NAD+
25°C, pH 8, mutant enzyme F16Q/C81S/N85R, activated by fructose 1,6-diphosphate
23
NAD+
25°C, pH 8, mutant enzyme F16Q/I37K/D38SC81S/N85R, activated by fructose 1,6-diphosphate
32
NAD+
25°C, pH 8, wild-type enzyme, activated by fructose 1,6-diphosphate
1293
phenylpyruvate
mutant I229A, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
6467
phenylpyruvate
wild-type, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
17479
phenylpyruvate
mutant Q88R, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
21.1
pyruvate
-
pH 6.0, 25°C, recombinant wild-type enzyme in presence of fructose 1,6-bisphosphate
178.4
pyruvate
-
pH 6.0, 25°C, recombinant mutant D38R in presence of fructose 1,6-bisphosphate
194.9
pyruvate
-
pH 6.0, 25°C, recombinant mutant D38R in absence of fructose 1,6-bisphosphate
250
pyruvate
pH 6.0, 25°C, recombinant wild-type enzyme
327.2
pyruvate
-
pH 6.0, 25°C, recombinant wild-type enzyme in absence of fructose 1,6-bisphosphate
1300
pyruvate
pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
1500
pyruvate
pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
1600
pyruvate
pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
1800
pyruvate
pH 5.5, temperature not specified in the publication, wild-type and mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
1800
pyruvate
pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
additional information
additional information
-
turnover-numbers for mutant enzymes with enlarged loop
-
additional information
pyruvate
-
the enzyme shows hyperbolic dependence on the substrate concentration
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
200
NADH
pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate
1200
NADH
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate
1400
NADH
pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
4400
NADH
pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
6800
NADH
pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
9000
NADH
pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
9000
NADH
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
13000
NADH
pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
507
phenylpyruvate
mutant I229A, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
1848
phenylpyruvate
wild-type, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
9397
phenylpyruvate
mutant Q88R, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
15
pyruvate
pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate
59
pyruvate
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, without fructose-1,6-bisphosphate
390
pyruvate
pH 7.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
480
pyruvate
pH 7.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
610
pyruvate
pH 7.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
790
pyruvate
pH 5.5, temperature not specified in the publication, mutant D241N LDH-2, with 3 mM fructose-1,6-bisphosphate
810
pyruvate
pH 5.5, temperature not specified in the publication, wild-type LDH-2, with 3 mM fructose-1,6-bisphosphate
1700
pyruvate
pH 5.5, temperature not specified in the publication, LDH-1, with 3 mM fructose-1,6-bisphosphate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.4
(benzylamino)(oxo)acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0025 - 0.016
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
0.0002 - 0.013
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
0.003
2,3-dihydroxy-6-methyl-7-(2-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0002
2,3-dihydroxy-6-methyl-7-(3-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.00003
2,3-dihydroxy-6-methyl-7-(4-methylbenzyl)-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.00059 - 0.00252
3-[7-(2,4-dimethoxypyrimidin-5-yl)-3-sulfamoylquinolin-4-yl]aminobenzoic acid
0.001
7-(4-chlorobenzyl)-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0002 - 0.0007
7-benzyl-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
0.0012 - 0.0013
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
0.0008
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl acetate
0.0006
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl butanoate
0.0003
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl pentanoate
0.0011
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl propanoate
0.0004 - 0.0006
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
10
oxo(phenylamino)acetic acid
-
above, LDH-A, pH not specified in the publication, temperature not specified in the publication
7
oxo[(2-phenylethyl)amino]acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
10
oxo[(2-phenylpropyl)amino]acetic acid
-
above, LDH-A, pH not specified in the publication, temperature not specified in the publication
0.9
oxo[(3-phenylpropyl)amino]acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.8
oxo[(4-phenylbutan-2-yl)amino]acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
2
oxo[(4-phenylbutyl)amino]acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
1
[(4-chlorobenzyl)amino](oxo)acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
2
[(4-methylbenzyl)amino](oxo)acetic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0025
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.016
1-[7-[3,4-dihydroxy-2-imino-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-8-yl]-2,3,8-trihydroxy-6-methyl-4-(propan-2-yl)naphthalen-1-yl]ethanone
-
pH not specified in the publication, temperature not specified in the publication
0.004
2,3-dihydroxy-4,6,7-trimethylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.013
2,3-dihydroxy-4,6,7-trimethylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.022
2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.034
2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.001
2,3-dihydroxy-6,7-dimethyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.002
2,3-dihydroxy-6,7-dimethyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0001
2,3-dihydroxy-6,7-dimethyl-4-propylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0001
2,3-dihydroxy-6,7-dimethyl-4-propylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0002
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.013
2,3-dihydroxy-6-methyl-4-(propan-2-yl)-7-[4-(trifluoromethyl)benzyl]naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.002
2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.003
2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.001
2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.006
2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00059
3-[7-(2,4-dimethoxypyrimidin-5-yl)-3-sulfamoylquinolin-4-yl]aminobenzoic acid
pH 7.5, 37°C, recombinant His-tagged enzyme, pyruvate reduction, competitive versus NADH
0.00252
3-[7-(2,4-dimethoxypyrimidin-5-yl)-3-sulfamoylquinolin-4-yl]aminobenzoic acid
pH 7.5, 37°C, recombinant His-tagged enzyme, pyruvate reduction, noncompetitive versus pyruvate
0.0005
7-benzyl-2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.008
7-benzyl-2,3-dihydroxy-4,6-dimethylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0002
7-benzyl-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0007
7-benzyl-2,3-dihydroxy-6-methyl-4-(propan-2-yl)naphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.00005
7-benzyl-2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0003
7-benzyl-2,3-dihydroxy-6-methyl-4-propylnaphthalene-1-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0012
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
-
pH not specified in the publication, temperature not specified in the publication
0.0013
8'-acetyl-1,1',6,6',7,7'-hexahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalene-8-carboxylic acid
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0008
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl acetate
-
pH not specified in the publication, temperature not specified in the publication
0.0008
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl acetate
-
pH not specified in the publication, temperature not specified in the publication
0.0006
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl butanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0006
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl butanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0003
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl pentanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0003
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl pentanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0011
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl propanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0011
8'-acetyl-8-cyano-1',6,6',7,7'-pentahydroxy-3,3'-dimethyl-5,5'-di(propan-2-yl)-2,2'-binaphthalen-1-yl propanoate
-
pH not specified in the publication, temperature not specified in the publication
0.0004
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
-
pH not specified in the publication, temperature not specified in the publication
0.0006
8-[8-acetyl-1,6,7-trihydroxy-3-methyl-5-(propan-2-yl)naphthalen-2-yl]-3,4-dihydroxy-7-methyl-5-(propan-2-yl)-2H-naphtho[1,8-bc]furan-2-one
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0007
gossypol
-
pH not specified in the publication, temperature not specified in the publication
0.0014
gossypol
-
LDH-B, pH not specified in the publication, temperature not specified in the publication
0.0019
gossypol
-
LDH-A, pH not specified in the publication, temperature not specified in the publication
0.0042
gossypol
-
LDH-C, pH not specified in the publication, temperature not specified in the publication
0.0116
gossypol
pH 5.5, 25°C, recombinant enzyme, with NADH and pyruvate
10.9
pyruvate
-
pH 6.0, 25°C, recombinant wild-type enzyme in presence of fructose 1,6-bisphosphate
31.1
pyruvate
-
pH 6.0, 25°C, recombinant mutant D38R in presence of fructose 1,6-bisphosphate
additional information
additional information
-
substrate and product inhibition kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00008
(benzylamino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.0083 - 0.179
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
0.00175 - 0.0114
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
0.0031 - 0.187
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
0.00051 - 0.0144
3-([3-carbamoyldimethoxypyrimidin-7-(2,4-dimethoxypyrimidin-5-yl)quinolin-4-yl]amino)benzoic acid
0.0011
3-hydroxy-1,2-oxazole-4-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.000039 - 0.0022
3-[7-(2,4-dimethoxypyrimidin-5-yl)-3-sulfamoylquinolin-4-yl]aminobenzoic acid
0.00065
4-hydroxy-1,2,5-oxadiazole-3-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.00014
4-hydroxy-1,2,5-thiadiazole-3-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.016
4-hydroxy-1,2-oxazole-3-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.191 - 0.225
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
0.0873 - 0.232
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
0.00005
cardiolipin
Sus scrofa
-
IC50: 0.00005 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
4.6
methylmalonate
Rattus norvegicus
-
IC50: 4.6 mM (enzyme from brain), 4.6 mM (enzyme from liver)
0.0001
oxo[(2-phenylethyl)amino]acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.000035
oxo[(3-phenylpropyl)amino]acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.0013
phosphatidylserine
Sus scrofa
-
IC50: 0.0013 mM, interaction with acidic phospholipids is most efficient at pH values below pH 6.5
0.00007
[(4-chlorobenzyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.00009
[(4-methylbenzyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.02
(abieta-8,11,13-trien-18-ylamino)(oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.059
(abieta-8,11,13-trien-18-ylamino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.16
(heptylamino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
(heptylamino)(oxo)acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
0.047
(hexylamino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.133
(hexylamino)(oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.088
(nonylamino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
(nonylamino)(oxo)acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0083
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.179
([2-cyano-4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.00175
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.0114
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]-2-methoxyphenyl]amino)(oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.0031
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.187
([4-[2-([5-hydroxy-2-[(4-methoxybenzyl)carbamoyl]-4-oxo-4H-chromen-8-yl]oxy)ethyl]phenyl]amino)(oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
1.7
3,5-dihydroxynaphthalene-2-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
150
3,5-dihydroxynaphthalene-2-carboxylic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
2.4
3,7-dihydroxynaphthalene-2-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
5
3,7-dihydroxynaphthalene-2-carboxylic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00051
3-([3-carbamoyldimethoxypyrimidin-7-(2,4-dimethoxypyrimidin-5-yl)quinolin-4-yl]amino)benzoic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme, L-lactate oxidation
0.0144
3-([3-carbamoyldimethoxypyrimidin-7-(2,4-dimethoxypyrimidin-5-yl)quinolin-4-yl]amino)benzoic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme, pyruvate reduction
0.000039
3-[7-(2,4-dimethoxypyrimidin-5-yl)-3-sulfamoylquinolin-4-yl]aminobenzoic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme, L-lactate oxidation
0.0022
3-[7-(2,4-dimethoxypyrimidin-5-yl)-3-sulfamoylquinolin-4-yl]aminobenzoic acid
Homo sapiens
pH 7.5, 37°C, recombinant His-tagged enzyme, pyruvate reduction
0.31
4,7-dibromo-3-hydroxynaphthalene-2-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
5.9
4,7-dibromo-3-hydroxynaphthalene-2-carboxylic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
4.6
6,6'-disulfanediyldipyridine-3-carboxylic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
6.6
6,6'-disulfanediyldipyridine-3-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.191
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.225
8-(2-[4-[(carboxycarbonyl)amino]-3-methoxyphenyl]ethoxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.52
8-(phenylamino)naphthalene-1-sulfonic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
1.1
8-(phenylamino)naphthalene-1-sulfonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0873
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.232
8-([4-[(carboxycarbonyl)amino]-3-methoxybenzyl]oxy)-5-hydroxy-4-oxo-4H-chromene-2-carboxylic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.0944
amino(oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.116
amino(oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
1.4
naphthalene-2,6-dicarboxylic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
5.11
naphthalene-2,6-dicarboxylic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
9.8
naphthalene-2,6-disulfonic acid
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
21
naphthalene-2,6-disulfonic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.15
oxo(pentadecylamino)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
oxo(pentadecylamino)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.041
oxo[(4-phenylbutyl)amino]acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.088
oxo[(4-phenylbutyl)amino]acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.0188
oxo[(tetrahydrofuran-2-ylmethyl)amino]acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
oxo[(tetrahydrofuran-2-ylmethyl)amino]acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
0.146
oxo[[1-(5,6,7,8-tetrahydronaphthalen-1-yl)ethyl]amino]acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
oxo[[1-(5,6,7,8-tetrahydronaphthalen-1-yl)ethyl]amino]acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
0.158
[(2-ethylphenyl)(phenyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
[(2-ethylphenyl)(phenyl)amino](oxo)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.014
[(2-methoxyethyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.025
[(2-methoxyethyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.035
[(3,3-diphenylpropyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.09
[(3,3-diphenylpropyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.031
[(3-methoxypropyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.043
[(3-methoxypropyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.157
[(3-methylbutyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
[(3-methylbutyl)amino](oxo)acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
0.0979
[(3-methylphenyl)(phenyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.107
[(3-methylphenyl)(phenyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.186
[(furan-2-ylmethyl)(methyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
[(furan-2-ylmethyl)(methyl)amino](oxo)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.043
[(naphthalen-1-ylmethyl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
[(naphthalen-1-ylmethyl)amino](oxo)acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
0.168
[benzyl(methyl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
[benzyl(methyl)amino](oxo)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.043
[bis(2-methylpiperidin-1-yl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
[bis(2-methylpiperidin-1-yl)amino](oxo)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.046
[bis(4-benzylpiperazin-1-yl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.169
[bis(4-benzylpiperazin-1-yl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.059
[bis(4-benzylpiperidin-1-yl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.101
[bis(4-benzylpiperidin-1-yl)amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.032
[bis(4-phenylpiperazin-1-yl)amino](oxo)acetic acid
Bos taurus
-
pH not specified in the publication, temperature not specified in the publication
0.2
[bis(4-phenylpiperazin-1-yl)amino](oxo)acetic acid
Plasmodium falciparum
-
above, pH not specified in the publication, temperature not specified in the publication
0.051
[[2-(4-bromophenyl)ethyl]amino](oxo)acetic acid
Plasmodium falciparum
-
pH not specified in the publication, temperature not specified in the publication
0.2
[[2-(4-bromophenyl)ethyl]amino](oxo)acetic acid
Bos taurus
-
above, pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.11
wild-type, pH 7.3, 55°C, presence of fructose-1,6-bisphosphate
0.58
mutant R157L, pH 7.3, 55°C, presence of fructose-1,6-bisphosphate
0.63
1.27
mutant R157L, lacking alcohol/aldehyde dehydrogenase gene AdhE, pH 7.3, 55°C, presence of fructose-1,6-bisphosphate
1.44
mutant R157L, lacking alcohol/aldehyde dehydrogenase gene AdhE, pH 7.3, 55°C
15.5
wild-type, substrate benzoylformic acid, pH 5.5, 30°C
16.48
substrate 3,4-dihydroxyphenylpyruvate, pH 6, 25°C
17.4
wild-type, substrate 4-hydroxyphenylpyruvate, pH 5.5, 30°C
2323
purified recombinant enzyme, pH 6.5, 55°C, pyruvate reduction
351
purified recombinant enzyme, pH 11.5, 55°C, lactate oxidation
4071
mutant Q88R, substrate phenylpyruvate, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
435.8
mutant I229A, substrate phenylpyruvate, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
451.5
mutant Q88R, substrate phenylpyruvate, pH 5.5, 30°C
512.4
mutant I229A, substrate phenylpyruvate, pH 5.5, 30°C
66.7
mutant T235G, substrate phenylpyruvate, pH 5.5, 30°C
671.2
wild-type, substrate oxaloacetic acid, pH 5.5, 30°C
680.3
mutant T235G, substrate phenylpyruvate, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
7.35
-
purified native aerobic control enzyme, pH 7.2, 25°C, pyruvate reduction
798
wild-type, substrate phenylpyruvate, presence of D-fructose-1,6-diphosphate, pH 5.5, 30°C
9.3 - 12.2
-
native enzyme in strain MG1363 at different growth phases and conditions, pH 7.0, 30°C
additional information
additional information
-
enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, overview
additional information
-
the enzyme shows hyperbolic dependence on the substrate concentration
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5.5
6.5
6.8
7.1
7.2
7.4
7.5
7.6
8.2
8.5
9.8
additional information
4.5
-
reduction of pyruvate, with addition of fructose 1,6-diphosphate and Mn2+
5.5
maximal activity at pH 5.5 which gradually decreases with the increase of pH
additional information
-
detailed kinetic analysis of enzyme mutant D241N, done at pH 5.5 and pH 7.5
additional information
detailed kinetic analysis of enzyme mutant D241N, done at pH 5.5 and pH 7.5
additional information
the enzyme also shows some activity in the absence of D-fructose-1,6-bisphosphate (FDP), with a pH optimum of pH 4.0. The addition of FDP results in a shift of pH optimum in pyruvate reduction, overview
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 9
-
activity range, the enzyme is inactive below pH 3.0 and above pH 9.0
4 - 7.5
4 - 8
over 40% of maximal activity for reduction of pyruvate within this range
5.2 - 7.2
5.3 - 8
-
pH 5.3: about 50% of maximal activity, pH 8.0: about 60% of maximal activity, reduction of pyruvate
5.4 - 10.8
Agama stellio stellio
-
pH 5.4: about 60% of maximal activity, pH 10.8: about 55% of maximal activity, reaction with pyruvate
5.5 - 8
-
pH 5.5: 40% of maximal activity of isoenzyme LDH-B4 and 60% of maximal activity of isoenzyme LDH-A2B2 and LDH-A4, pH 8.0: about 60% of maximal activity of isoenzyme LDH-A4, LDH-B4 and LDH-A4B4, reduction of pyruvate
6 - 8
Molinema dessetae
-
pH 6.0: 85% of maximal activity, pH 8.0: 45% of maximal activity, reduction of pyruvate
6.4 - 6.9
6.5 - 10
-
optimal pH range for pyruvate reduction and lactate oxidation is 6.5-7.0 and 9.0-10.0, respectively
6.6 - 10.8
Agama stellio stellio
-
pH 5.4: about 55% of maximal activity, pH 10.8: about 55% of maximal activity, reaction with lactate
7.7 - 9.5
-
pH 7.7: about 60% of maximal activity, pH 9.5: about 30% of maximal activity, reduction of pyruvate
8 - 9.5
20% of maximal activity for oxidation of lactate at pH 8.0, 90% at pH 8.5, and maximal activity at pH 8.5-9.5, inactive at pH 7.5
8 - 9.6
Molinema dessetae
-
pH 8.0: 60% of maximal activity, pH 9.6: 45% of maximal activity, oxidation of lactate
8.5 - 10.7
-
pH 8.5: about 60% of maximal activity, pH 10.7: about 70% of maximal activity, oxidation of lactate
additional information
4 - 7.5
activity range, inactive at pH 8.0, profile overview. High level of activity between pH 4.0 and pH 7.5
5.2 - 7.2
LDH activity shows a broad plateau between pH 5.2 and pH 7.2, and no activity at pH 4.8
5.2 - 7.2
-
pH 5.2: about 35% of maximal activity, pH 7.2: about 50% of maximal activity
additional information
the two isozymes LDH and LDHB exhibited different pH profiles for maximal activity
additional information
-
the two isozymes LDH and LDHB exhibited different pH profiles for maximal activity
additional information
under alkaline conditions the presence of the recombinant LDH protein increases the differentiation
additional information
under alkaline conditions the presence of the recombinant LDH protein increases the differentiation
additional information
-
under alkaline conditions the presence of the recombinant LDH protein increases the differentiation
additional information
under alkaline conditions the presence of the recombinant LDH proteins increases the differentiation
additional information
under alkaline conditions the presence of the recombinant LDH proteins increases the differentiation
additional information
-
under alkaline conditions the presence of the recombinant LDH proteins increases the differentiation
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
40
45
-
highest relative activity for both the reduction and oxidation reactions
50
55
recombinant enzyme, pyruvate reduction and lactate oxidation
additional information
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14 - 46
37 - 60
-
37°C: about 85% of maximal activity, 60°C: about 90% of maximal activity
37 - 65
-
optimal temperatures for the reduction and oxidation reactions are 37-65°C and 40-50°C, respectively
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a Gram-negative opportunistic pathogen found exclusively in the mammalian oral cavity in the space between the gums and the teeth known as the gingival crevice, gene AA02769
-
-
brenda
a Gram-negative opportunistic pathogen found exclusively in the mammalian oral cavity in the space between the gums and the teeth known as the gingival crevice, gene AA02769
-
-
brenda
Q5F885 i.e. oxidoreductase domain, Q5F884 i.e. LUD_dom domain-containing protein, Q5F883 i.e. (Fe-S)-binding protein
Q5F885; Q5F884; Q5F883
UniProt
brenda
Q5F885 i.e. oxidoreductase domain, Q5F884 i.e. LUD_dom domain-containing protein, Q5F883 i.e. (Fe-S)-binding protein
Q5F885; Q5F884; Q5F883
UniProt
brenda
isolated from Brassica rapa L. subsp. nipposinica (L.H. Bailey) Hanelt var. linearifolia
-
-
brenda
LDH-1; isolated from Brassica rapa L. subsp. nipposinica (L.H. Bailey) Hanelt var. linearifolia
UniProt
brenda
isolated from Brassica rapa L. subsp. nipposinica (L.H. Bailey) Hanelt var. linearifolia
-
-
brenda
LDH-1; isolated from Brassica rapa L. subsp. nipposinica (L.H. Bailey) Hanelt var. linearifolia
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the level of L-lactate dehydrogenase B are specifically increased in non-small cell lung cancer
brenda
lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
brenda
lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
brenda
-
brain metastatic subline of NCI-H226. L-lactate dehydrogenase B is significantly up-regulated in the conditional medium of NCI-H226Br cells
brenda
-
activities of both H- and M-isoforms of LDH are high but neurons show a dominance of H-isoform activity
brenda
lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
brenda
-
patients with tubercular pyothorax show highest levels in LDH-5 followed by LDH-4, LDH-3, LDH-2 and LDH-1
brenda
lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
brenda
-
patients with tubercular pyothorax show highest levels in LDH-5 followed by LDH-4, LDH-2, LDH-3 and LDH-1. In LDH-5 and LDH-4 nearly 4- and 5folds increase in patients
brenda
additional information
contains a skeletal muscle type and heart type mixed heterotetrameric enzyme, H2M2
brenda
normal and malignant human breast tissues. The enzyme is highly expressed in breast
brenda
-
differential expressions of LDH isozymes in different types of tumors
brenda
-
differential expressions of LDH isozymes in different types of tumors
-
brenda
-
FBP-activated L-nLDH activity is constantly very significant throughout the growth period, even when lactate is consumed in the stationary phase of respiration. During the lactate utilization period, L-nLDH activity is regulated by some factors and the pyruvate reduction activity is completely inhibited or masked
brenda
Lactococcus cremoris MG1363
-
FBP-activated L-nLDH activity is constantly very significant throughout the growth period, even when lactate is consumed in the stationary phase of respiration. During the lactate utilization period, L-nLDH activity is regulated by some factors and the pyruvate reduction activity is completely inhibited or masked
-
brenda
steady-state growth at pH 7 and pH 5
brenda
-
in patients with tubercular pyothorax, decrease in heart specific aerobic LDH-1 (6fold), LDH-2 (2fold) and LDH-3 (1.5fold)
brenda
-
significant rise in the level of muscle specific anaerobic LDH-5 and LDH-4 in patients with tubercular pyothorax
brenda
contains a skeletal muscle type homotetrameric enzyme, M4
brenda
additional information
structural features for structural stability, comparison to enzymes from other species in extreme environments
brenda
additional information
-
structural features for structural stability, comparison to enzymes from other species in extreme environments
brenda
additional information
structural features for structural stability, comparison to enzymes from other species in extreme environments
brenda
additional information
-
structural features for structural stability, comparison to enzymes from other species in extreme environments
brenda
additional information
LDH is stage specifically transcribed in Eimeria, but its presence at the protein level remains constant during different life-cycle stages
brenda
additional information
-
LDH is stage specifically transcribed in Eimeria, but its presence at the protein level remains constant during different life-cycle stages
brenda
additional information
-
homo- and heterotetrameric isozymes with tissue-specific expression
brenda
additional information
serum LDH is commonly increases in patients with hematopoietic malignancies, such as Hodgkin's lymphoma, non-Hodgkin's lymphoma, or multiplemyeloma
brenda
additional information
-
in satellite gliocytes, activities of both H- and M-isoforms of LDH are high, dominance of M-isoform activity
brenda
additional information
-
type-I isolate, e.g. strain NRRL 395, accumulating primarily lactic acid when grown in the presence of a fermentable carbon source and containing two LDH genes, ldhA and ldhB, and type-II isolates, e.g. strain 99-880, synthesizing predominantly fumaric acid and having only an ldhB gene
brenda
additional information
-
metabolic adaptation of Staphylococcus aureus to nitrosative stress, overview
brenda
additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
brenda
additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
brenda
additional information
-
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
brenda
additional information
-
surface of the tegument in adults. Is absent from internal tissues
brenda
additional information
structural features for structural stability, comparison to enzymes from other species in extreme environments
brenda
additional information
-
structural features for structural stability, comparison to enzymes from other species in extreme environments
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
inner compartment, transport and metabolism of L-lactate, overview
brenda
-
L-lactate dehydrogenase is restricted to the inner mitochondrial compartments
brenda
-
LDH is present in the inner mitochondrial compartments
brenda
additional information
-
no signal peptide sequences and transmembrane domains are contained in LDH sequence
-
brenda
additional information
-
immunohistochemic analysis of subcellular localization
-
brenda
additional information
the subcellular localization of LDH-5 appears to be dependent on the phosphorylation state of Y238
-
brenda
additional information
-
the recombinant protein is exclusively associated with inclusion bodies
-
brenda
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
sequence identity between the Enterococcus mundtii LDH-1 and LDH-2 is 44.9%
evolution
-
genes ldh, ldhB and ldhX, are transcribed to some extent in Lactococcus lactis strain MG1363. The product of the ldhX gene has little nLDH activity as well as ldhB which exhibits only leaky transcription and plays a minor role in lactate yield. LDHA encoded by ldh has been found to perform major L-nLDH activity, with the contribution of other alternate L-nLDHs being small
evolution
there are two types of L-nLDHs, non-allosteric L-nLDHs and allosteric L-nLDHs
evolution
-
there are two types of L-nLDHs, non-allosteric L-nLDHs and allosteric L-nLDHs
-
evolution
-
sequence identity between the Enterococcus mundtii LDH-1 and LDH-2 is 44.9%
-
evolution
Lactococcus cremoris MG1363
-
genes ldh, ldhB and ldhX, are transcribed to some extent in Lactococcus lactis strain MG1363. The product of the ldhX gene has little nLDH activity as well as ldhB which exhibits only leaky transcription and plays a minor role in lactate yield. LDHA encoded by ldh has been found to perform major L-nLDH activity, with the contribution of other alternate L-nLDHs being small
-
malfunction
loss of water-forming NADH oxidase NOX activity in Streptococcus mutans leads to Rex-mediated overcompensation in NAD+ regeneration by lactate dehydrogenase. The altered transcriptome and metabolome of the DELTAnox strain are sufficient to impair its ability to compete with commensal peroxigenic oral streptococci during growth under aerobic conditions, phenotype, overview
malfunction
LDH-5 inhibitors decrease mitochondrial membrane potential and elevate intracellular oxidative stress that diminishes the ability of cells to proliferate, reduces their metastatic potential, and increases sensitivity to chemotherapeutic drugs. Inhibitors can also act as a blocker of the LDH-5ssDNA interactions to prevent RNA synthesis. miR-34a is a direct repressor of LDHA gene expression. Inhibiting LDHA expression may reduce the invasive and metastatic potential of cancer cells by decreasing their proliferation ability and reversing their resistance to chemotherapy. Enzyme inhibitors NHI-1 and -2 used together with gemcitabine enhance the antiproliferative and anti-invasive activities of the chemotherapeutic drug, under both normoxia and hypoxia, in pancreatic ductal adenocarcinoma (PDAC) cell lines. Inhibitor NIH-2, combined with the redox-dependent bioreductive anticancer prodrug EO9, synergistically induces p53-positive cancer cell death
malfunction
silencing LDHB selectively inhibits the proliferation of both oxidative and glycolytic cancer cells over normal cells, targeting LDHB selectively blocks autophagy in oxidative and glycolytic cancer cells, but siLDHB does not affect the subcellular distribution pattern of lysosomes and their distance to the cell nucleus. siLDHB induces lysosomal inhibition in oxidative cancer cells. Overexpression of LDHB decreases the number of acidic vesicles per cell. LDHB overexpression increases mature autolysosome formation and intracellular proteolysis in SiHa and in HeLa cells. LDHB reaction substrate lactate and product pyruvate do not metabolically restore autophagy and intracellular proteolysis in LDHB-depleted SiHa cells, but LDHB-depleted cells switch to a glycolytic metabolism
malfunction
-
loss of water-forming NADH oxidase NOX activity in Streptococcus mutans leads to Rex-mediated overcompensation in NAD+ regeneration by lactate dehydrogenase. The altered transcriptome and metabolome of the DELTAnox strain are sufficient to impair its ability to compete with commensal peroxigenic oral streptococci during growth under aerobic conditions, phenotype, overview
-
metabolism
-
the enzyme catalyzes the first step in L-lactate catabolism
metabolism
-
LDH plays a central role in several metabolic pathways, e.g. in energy production in glycolysis, in gluconeogenesis. Glycolytic process, overview
metabolism
-
L-lactate dehydrogenase is an important enzyme involved in the last step of glycolysis that catalyzes the reversible conversion of pyruvate to L-lactate with the simultaneous oxidation of NADH to NAD+
metabolism
-
NAD-dependent lactate dehydrogenase catalyses the first step in respiratory utilization of lactate by Lactococcus lactis
metabolism
NAD-dependent L-lactate dehydrogenases (L-nLDHs) catalyze the last step of anaerobic glycosis, the reduction of pyruvate to L-lactate, concomitantly oxidizing NADH into NAD+
metabolism
lactate dehydrogenase-5 (LDH-5) is a central player in theWarburg effect which catalyzes the formation of lactate in the final step of the glycolytic pathway
metabolism
lactate dehydrogenase (LDH) is a glycolytic enzyme that catalyzes the final step of glycolysis and produces NAD+
metabolism
-
since the mitochondrial metabolism of (S)-lactate results in synthesis and export of oxaloacetate, malate and citrate into the extramitochondrial phase, an anaplerotic role for the mitochondrial (S)-lactate metabolism is proposed
metabolism
the substrate binding and product states are stabilized only in the open-loop conformation of LDH and the reaction occurs in the closed-loop conformation, i.e., before and after the chemical reaction, a large-scale structural transition from the open-loop conformation to the closed-loop conformation and vice versa occurs. The closed-loop conformation stabilizes the transition state of the reaction. In contrast, the open-loop conformation stabilizes the substrate binding and final states
metabolism
LDH activity with free NADH and GAPDH-NADH complex always take place in parallel. NADH-channeling from D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to L-lactate dehydrogenase (LDH) is observed only in assays that mimic cytosolic conditions where free NADH concentration is negligible and the GAPDH-NADH complex is dominant. LDH and GAPDH can form a leaky channeling complex only at the limiting NADH concentrations. A positive electric field between the NAD(H) binding sites on LDH and GAPDH tetramers can merge in the LDH-GAPDH complex
metabolism
L-lactate dehydrogenase (LDHA) is a substrate of protein tyrosine phosphatase PTP1B. LDHA enrichment ias significantly lower in PTP1B knockdown cell lysate compared to untreated and scrambled siRNA controls
metabolism
-
predominantly the conformational changes in the T to R transition start from the region near the active site, comprised of helix alphaC, helix alpha1/2G, helix alpha3G, and helix alpha2F, and proceed to other structural units, thus completing the global motion. The bottleneck for assembly is the formation of the correct orientational registry between the subunits, requiring contacts between the interface residues. These residues are part of the allostery wiring diagram
metabolism
-
the enzyme catalyzes the first step in L-lactate catabolism
-
metabolism
-
NAD-dependent L-lactate dehydrogenases (L-nLDHs) catalyze the last step of anaerobic glycosis, the reduction of pyruvate to L-lactate, concomitantly oxidizing NADH into NAD+
-
metabolism
Lactococcus cremoris MG1363
-
NAD-dependent lactate dehydrogenase catalyses the first step in respiratory utilization of lactate by Lactococcus lactis
-
metabolism
-
predominantly the conformational changes in the T to R transition start from the region near the active site, comprised of helix alphaC, helix alpha1/2G, helix alpha3G, and helix alpha2F, and proceed to other structural units, thus completing the global motion. The bottleneck for assembly is the formation of the correct orientational registry between the subunits, requiring contacts between the interface residues. These residues are part of the allostery wiring diagram
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physiological function
-
LADH-A is a key enzyme that couples L-lactate production to reoxidation of NADH formed during glycolysis
physiological function
-
the enzyme catalyzes the stereospecific conversion of lactate to pyruvate and converts NAD+ to NADH, which is an important way of regenerating NAD+, enabling the continuation of glycolysis
physiological function
-
although Ldh-2 contributes to lactate production, Ldh-1 plays the major role in energy metabolism in Enterococcus faecalis
physiological function
-
the parasite's ATP production is almost completely dependent on the glucose metabolism and the glycolytic pathway, that is absent in normal human host cells, overview. PfLDH plays the essential role in NAD+ regenration needed for the continuity of the glycolytic cycle
physiological function
-
Inactivation of the lactate dehydrogenase gene results in a metabolic shift predominantly towards ethanol production. Formic and acetic acids are still produced, the latter in lower amounts than with the wild-type, but, unlike the wild-type strain, significant quantities of pyruvic acid accumulate
physiological function
alternative allosteric regulation mechanism of an acidophilic L-lactate dehydrogenase, overview. LDH-1 mainly plays a role in L-lactate production in Enterococcus mundtii, while LDH-2 plays another, different role
physiological function
the stereospecific L-LDH is a fructose 1,6-diphosphate-activated NAD-dependent lactate dehydrogenase, L-nLDH
physiological function
lactate dehydrogenase (LDH) is a critical enzyme during aerobic glycolysis as it is typically responsible for the production of lactate and regeneration of NAD+, which allows for the continued functioning of glycolysis even in the absence of oxygen. LDH is the final enzyme in glycolysis pathway that catalyzes interconversion of pyruvate and lactate and it also regenerates NAD+, which is necessary for continued high glycolysis rate in cancer cells
physiological function
lactate dehydrogenase 5 (LDH-5) catalyzes the reduction of pyruvate by NADH to form lactate, thus determining the availability of NAD+ to maintain the continuity of glycolysis.Direct phosphorylation of LDHA at Y10 and Y83 strongly enhances LDH-5 tetramer formation and cofactor binding, resulting in significantly increased LDH enzymatic activity and promoting cancer cell metabolism and tumor growth. LDH-5 tyrosine phosphorylation might be an extra regulatory mechanism underlying the Warburg effect and lactate production. LDHA tyrosine phosphorylation decides about the translocation of LDH-5 to the nucleus, where it acts as a single-stranded DNA-binding protein, stimulating transcription and/or DNA replication. LDH-5 plays a crucial role in tumor maintenance and elevated LDHA gene expression characterizes many human tumors
physiological function
lactate dehydrogenase B (LDHB), catalyzing the conversion of lactate and NAD+ to pyruvate, NADH and H+, controls lysosomal acidification, vesicle maturation, and intracellular proteolysis. LDHB activity is necessary for basal autophagy and cancer cell proliferation not only in oxidative cancer cells but also in glycolytic cancer cells. Lactate supports lysosomal acidification and autophagy in cancer. Lactate oxidation by LDHB yields protons that fuel lysosomal V-ATPase. LDHB is critical for lysosomal activity and autophagy in cancer cells. LDHB controls early tumor progression and the number of cancer cells, and negatively affects patient survival. Lactate promotes LDHB-dependent autophagy in oxidative cancer cells
physiological function
-
lactate dehydrogenase is the terminal enzyme of anaerobic glycolysis, and has a crucial role in sustaining ATP production by glycolysis during periods of anoxia via regenerating NAD+ through the production of lactate. Anoxia-induced modifications of crayfish muscle LDH may contribute significantly to modulating enzyme function under anoxic conditions
physiological function
-
both the single-gene deletion mutants of isoforms LDHL1 or LDHL2 exhibit phenotypic defects in vegetative growth, sporulation, spore germination, L-lactate biosynthesis and activity. The two L-lactate dehydrogenases are involved in the utilization of carbon sources and maintenance of redox homeostasis during spore germination. The LDHL1 deletion mutant exhibits reduced virulence on wheat spikelets and on corn stigmas
physiological function
Q5F885; Q5F884; Q5F883
the growth of the LutACB mutants is similar to that of the wild-type strain on L-lactate. The isoforms LutACB/LldD double mutant fails to grow on L-lactate, and complementation of this strain with LutACB restores growth to wild-type levels. LutACB contributes to L-lactate dehydrogenase activity under iron-replete conditions, and the LutACB deletion mutant is impaired in its ability to survive within human primary cervical epithelial cells
physiological function
-
lactate can fuel the bioenergetics of heart, muscle, and liver mitochondria. Lactate is just as effective as pyruvate at stimulating mitochondrial coupling efficiency. Inclusion of LDH and pyruvate dehydrogenase inhibitors abolishes respiration in mitochondria energized with lactate. Lactate also fueled mitochondrial ROS generation and is just as effective as pyruvate at stimulating H2O2 production. Lactate-induced ROS production is inhibited by both LDH and PDH inhibitors
physiological function
-
both the single-gene deletion mutants of isoforms LDHL1 or LDHL2 exhibit phenotypic defects in vegetative growth, sporulation, spore germination, L-lactate biosynthesis and activity. The two L-lactate dehydrogenases are involved in the utilization of carbon sources and maintenance of redox homeostasis during spore germination. The LDHL1 deletion mutant exhibits reduced virulence on wheat spikelets and on corn stigmas
-
physiological function
-
Inactivation of the lactate dehydrogenase gene results in a metabolic shift predominantly towards ethanol production. Formic and acetic acids are still produced, the latter in lower amounts than with the wild-type, but, unlike the wild-type strain, significant quantities of pyruvic acid accumulate
-
physiological function
-
the stereospecific L-LDH is a fructose 1,6-diphosphate-activated NAD-dependent lactate dehydrogenase, L-nLDH
-
physiological function
-
alternative allosteric regulation mechanism of an acidophilic L-lactate dehydrogenase, overview. LDH-1 mainly plays a role in L-lactate production in Enterococcus mundtii, while LDH-2 plays another, different role
-
physiological function
-
the growth of the LutACB mutants is similar to that of the wild-type strain on L-lactate. The isoforms LutACB/LldD double mutant fails to grow on L-lactate, and complementation of this strain with LutACB restores growth to wild-type levels. LutACB contributes to L-lactate dehydrogenase activity under iron-replete conditions, and the LutACB deletion mutant is impaired in its ability to survive within human primary cervical epithelial cells
-
additional information
-
ldhA expression is primarily repressed by SugR in the absence of sugar. In the presence of sugar, SugR-mediated repression of ldhA is alleviated, and ldhA expression is additionally enhanced by LldR inactivation in response to L-lactate produced by LdhA
additional information
-
the ldh-1 mutants detoxifies excess pyruvate by converting it to acetoin
additional information
-
the enzyme is involved in development of cancer, especially of hypoxic cancer cells, since the cancer cells relay on LDH-A for the energy supply. The glycolytic phenotype is responsible for the tumorigenicity of hypoxic cells
additional information
the key catalytic residues Arg109, Asp168, Arg171, and His 195, are conserved in Bacillus coagulans strain NL01 L-nLDH
additional information
-
the key catalytic residues Arg109, Asp168, Arg171, and His 195, are conserved in Bacillus coagulans strain NL01 L-nLDH
-
Show AA Sequence and Transmembrane Helices (13144 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
134000
140000
34600
-
x * 39000, recombinant His6-tagged LDH-1, SDS-PAGE, x * 34600, about, sequence calculation
35000
36000
39000
42000
-
x * 42000, recombinant His6-tagged LctD, SDS-PAGE
130000
-
tetramer, sucrose density gradient centrifugation in presence of fructose 1,6-diphosphate and NADH
35000
-
8 * 35000, enzyme also exists in an tetrameric enzyme form, SDS-PAGE, meniscus depletion experiments in 4 M guanidinium chloride
39000
-
x * 39000, recombinant His6-tagged LDH-1, SDS-PAGE, x * 34600, about, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotetramer
the heterotetrameric LDH (H2M2) from swine brain is formed by two subunit of LDHA and two subunits of LDHB
homotetramer
octamer
-
8 * 35000, enzyme also exists in an tetrameric enzyme form, SDS-PAGE, meniscus depletion experiments in 4 M guanidinium chloride
tetramer
additional information
?
-
x * 42000, recombinant His6-tagged LctD, SDS-PAGE
-
?
-
x * 35500, isoform LDHL1, calculated from sequence and SDS-PAGE
?
-
x * 34400, isoform LDHL2, calculated from sequence and SDS-PAGE
?
Sporolactobacillus inulinus YBS1-5
-
x * 35500, isoform LDHL1, calculated from sequence and SDS-PAGE
-
?
Sporolactobacillus inulinus YBS1-5
-
x * 34400, isoform LDHL2, calculated from sequence and SDS-PAGE
-
?
-
x * 39000, recombinant His6-tagged LDH-1, SDS-PAGE, x * 34600, about, sequence calculation
homotetramer
each monomer has one active site, and the tetramer has two allosteric sites, each of which is situated at the Y-axis interface between two monomers
homotetramer
-
each monomer has one active site, and the tetramer has two allosteric sites, each of which is situated at the Y-axis interface between two monomers
-
homotetramer
-
dimer of dimers, differential chemical crosstalk between the monomers
tetramer
-
wild-type enzyme and N-terminal deletion mutants lacking the first 5 or the first 10 amino acids
additional information
molecular modeling of the three-dimensional enzyme structure in comparison to the enzyme structure from Iguana iguana, overview
additional information
-
molecular modeling of the three-dimensional enzyme structure in comparison to the enzyme structure from Iguana iguana, overview
additional information
-
analysis of enzyme structure under high pressure conditions: even the lowest high pressure processing treatment of 206 MPa induces a reduction in LDH activity, and the course of reduction increases with high pressure processing treatment until complete inactivation at 482, 515, and 620 MPa. The structure of LDH shows gradual denaturation after exposure at 206 MPa for 6 min, leading to a random coil structure at both 515 and 620 MPa. The loss of LDH activity with increasing pressure and time treatment was due to the combined effects of denaturation and aggregation, structure analysis by far-ultraviolet circular dichroism spectroscopy and dynamic light scattetering
additional information
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview
additional information
-
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview
additional information
the ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analog in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: lactate, pyruvate or oxamate
additional information
-
the ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analog in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: lactate, pyruvate or oxamate
additional information
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from crystal structure, overview
additional information
-
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from crystal structure, overview
additional information
-
secondary, tertiary, and quaternary structure analysis, and structure comparisons, overview.The subunit structure of L-LDH can be divided into N-terminal NADH-binding domain and C-terminal catalytic domain
additional information
secondary, tertiary, and quaternary structure analysis, and structure comparisons, overview.The subunit structure of L-LDH can be divided into N-terminal NADH-binding domain and C-terminal catalytic domain
additional information
-
secondary, tertiary, and quaternary structure analysis, and structure comparisons, overview.The subunit structure of L-LDH can be divided into N-terminal NADH-binding domain and C-terminal catalytic domain
-
additional information
three-dimensional structure models of eLDHA monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i10, overview
additional information
three-dimensional structure models of eLDHA monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i10, overview
additional information
-
three-dimensional structure models of eLDHA monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i10, overview
additional information
three-dimensional structure models of eLDHB monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i0z, overview
additional information
three-dimensional structure models of eLDHB monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i0z, overview
additional information
-
three-dimensional structure models of eLDHB monomeric and tetrameric proteins are constructed by homology modeling, structure analysis and comparison to the human enzymes, PDB accession number 1i0z, overview
additional information
-
binary complex of LDH with the cofactor NADH and the LDH/NADH-oxamate ternary complex, molecular dynamics, and simulation model from crystal structure at 2.1 A resolution, Protein DataBank entry 1IOZ, overview
additional information
-
structure comparison of LDH-M and LDH-H subunit isoforms, the homotetramers have essentially the same tertiary structure, while the hybrid tetramers show different structures, overview. Rossmann fold topology, structure comparison to the enzyme from Plasmodium falciparum, PDB IDs 1i10 and 1ldg, Ser163 is a highly conserved residue amongst human hLDH isozymes, corresponds to Leu163 in PfLDH, differences occur mainly in the N-terminus, overview
additional information
molecular modeling of the three-dimensional enzyme structure in comparison to the enzyme structure from Amblyrhynchus cristatus, overview
additional information
-
molecular modeling of the three-dimensional enzyme structure in comparison to the enzyme structure from Amblyrhynchus cristatus, overview
additional information
LDH has a slightly larger negative charge than LDHB and a greater concentration of positive charges at the interface between monomers
additional information
-
LDH has a slightly larger negative charge than LDHB and a greater concentration of positive charges at the interface between monomers
additional information
-
LDH has a slightly larger negative charge than LDHB and a greater concentration of positive charges at the interface between monomers
-
additional information
-
three bands detected after SDS-PAGE with MW of 60000 Da, 66000 Da and 74000 Da
additional information
-
three-dimensional structures of the L-LDH-NADH complex of enzyme from muscle and heart, molecular analysis, overview
additional information
-
Rossmann fold topology, structure comparison to the enzyme from Homo sapiens, PDB IDs 1i10 and 1ldg, differences occur mainly in the N-terminus, overview
additional information
-
enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, overview
additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA is the skeletal muscle type, M, isozyme, and LDHB is the heart type, H, isozyme
additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA is the skeletal muscle type, M, isozyme, and LDHB is the heart type, H, isozyme
additional information
-
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA is the skeletal muscle type, M, isozyme, and LDHB is the heart type, H, isozyme
additional information
TeLdhL contains a GXGXXG motif common to most NAD-linked dehydrogenases close to the N-terminus, and a putative signal peptide with cleavage site between residue 26 and 27, deletion of the putative signal peptide sequence leads to nonexpression of TeLdhL
additional information
-
TeLdhL contains a GXGXXG motif common to most NAD-linked dehydrogenases close to the N-terminus, and a putative signal peptide with cleavage site between residue 26 and 27, deletion of the putative signal peptide sequence leads to nonexpression of TeLdhL
-
additional information
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview
additional information
-
primary sequence, tertiary structure modelling, analysis of the apo form and ternary complexes from cyrstal structure, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acylation
lysine acetylation appears as a specific modification of LDH-5. It is involved in the control of its activity. Acetylation at Y5 decreases the LDHA protein level and inhibits LDH-5 activity. Lysine-5 acetylation reduces and be accompanied with increased LDHA protein levels in both early and late stages of pancreatic cancers. Acetylated LDHA can be recognized by a cytosolic chaperone and it is easily degraded by lysosomal proteolysis
phosphoprotein
phosphoprotein
-
purified LDH from aerobic control crayfish shows significantly higher amounts of serine/threonine phosphorylation than does the anoxic enzyme form
phosphoprotein
LDH-5 can serve as a substrate of the oncogenic viral Src (v-Src) tyrosine kinase and the oncogenic receptor tyrosine kinase FGFR1. Direct phosphorylation of LDHA at Y10 and Y83 strongly enhances LDH-5 tetramer formation and cofactor binding, resulting in significantly increased LDH enzymatic activity. LDHA tyrosine phosphorylation also decides about the translocation of LDH-5 to the nucleus
phosphoprotein
L-lactate dehydrogenase (LDHA) is a substrate of protein tyrosine phosphatase PTP1B
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified His-tagged wild-type and mutant H171C enzymes, hanging drop vapor diffusion method, 0.002 ml of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.5, with 1 mM fructose 1,6-bisphosphate and NAD+, is mixed with 0.002 ml of reservoir solution containing 16% w/v PEG MME 2000, 0.06 M sodium/potassium phosphate, 1.8% v/v glycerol pH 5.5, or 14% w/v PEG 4000, 0.1 M sodium/potassium phosphate, 2% v/v glycerol, pH 7.0, equilibration against 1 ml reservoir solution, X-ray diffraction structure determinaation and analysis at 2.2-2.5 A resolution
-
apo enzyme form, X-ray diffraction structure determination and analysis at 2.35 A resolution, molecular replacement
purified recombinant enzyme as apo-enzyme and in four ternary complexes, The ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analogue in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: lactate, pyruvate or oxamate. X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution
purified enzyme, hanging drop vapor diffusion technique, 8 mg/ml protein in 20% PEG 5000 MME, 0.1M bicine, pH 9.0, at room temperature, X-ray diffraction structure determination and analysis at 2.5 A resolution, molecular replacement
purified recombinant wild-type enzyme, in apoform and in complex with fructose-1,6-bisphosphate and NADH, X-ray diffraction structure determination and analysis at 2.38 A and 2.30 A resolution, respectively, modelling
crystal structure of a mutant into which an additional loop has been engineered in order to prevent tetramerization
-
binary complex of LDH with the cofactor NADH and the LDH/NADH-oxamate ternary complex, molecular dynamics, and simulation model from crystal structure at 2.1 A resolution, Protein DataBank entry 1IOZ, overview
-
lactate dehydrogenase A in apo form, in ternary complex with oxalate and kanamycin, and in inhibitor-bound form, hanging drop vapour diffusion method, apo-LDHA crystals are grown by mixing of 0.002 ml of 25 mg/ml enzyme protein with 0.002 ml reservoir solution consisting of 100 mM Bis-Tris propane, pH 7.0, 20% v/v PEG 400, and 100 mM LiCl. LDHA-NADH crystals are grown by first incubating 25 mg/ml enzyme protein with 3 mM NADH for 2 h at 4°C and then setting up 0.004 ml drops with a 2:1:1 volume ratio of LDHA-NADH, reservoir solution, containing 18% w/v PEG 3350, and 50 mM HEPES, pH 6.8, and another reagent containing 0.16% w/v L-citrulline, 0.16% w/v L-ornithine hydrochloride, 0.16% w/v urea, 0.16% w/v oxalic acid, 0.16% w/v kanamycin monosulfate, and 0.16% w/v L-arginine in 0.02 M HEPES sodium, pH 6.8, 20°C. Apo and NADH-bound LDHA crystals appear after three weeks. LDHA-inhibitor complex crystals are obtained by adding 0.010 ml soaking solution containing 20 mM inhibitor, 100 mM HEPES, pH 7.5, 50 mM LiCl, 100 mM bis-tris propane pH 7.0, 20% v/v DMSO, and 25% PEG 8000, to 0.002 ml hanging drops containing apo LDHA crystals and allowing the crystals to sit at room temperature for 24 h, X-ray diffraction structure determination and analysis at 2.1-3.2 A resolution, molecular replacement method using model structure PDB ID1i10
hanging drop method of vapour diffusion, ternary complex with NADH and oxamate
-
crystals the apo-form of PfLDH are ontained by hanging-drop method with 2-methyl-2,4-pentanediol as precipitant, crystallization of enzyme:naphthoic acid complexes with 2,6-naphthalenedicarboxalic acid, 2,6-naphthalene disulfonic acid or 3,7-dihydroxy naphthalene-2-carboxylic acid and 3,7-dihydroxy naphthalene-2-carboxylic acid plus NAD+
-
purified recombinant His-tagged Sa-LDH-1, sitting drop vapour diffusion method, 0.001 ml protein solution, containing 5 mg/ml protein in 20 mM Tris-HCl, 200 mM NaCl, pH 7.5, is mixed with mixed with an equal volume of reservoir solution, containing ,0.2 M calcium chloride dihydrate, 0.1 M Na HEPES, pH 7.5, 28%(v/v) PEG 400, and equilibrated against 0.1 ml reservoir solution, 3 days, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
2.1 A resolution as a quarternary complex with the cofactor NADH, the allosteric activator fructose-1,6-bisphosphate and the substrate analog oxamate
-
apo enzyme form and enzyme in ternary complex, X-ray diffraction structure determination and analysis at 2.1-2.3 A resolution, molecular replacement
in apo-form and in ternary complexes containing NAD+ or NAD+-analogue 3-acetylpyridine adenine dinucleotide and sulfate or the inhibitor oxalate
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A96L/N212K
mutation increases Km value and eliminates substrate inhibition
I283V |
site-directed mutagenesis, the mutation switches the nature of the residue from Amblyrhynchus cristatus to that of Iguana iguana, another Galapagos marine iguana, the mutation does not affect enzyme kinetics, overview
T9A
site-directed mutagenesis, the mutation switches the nature of the residue from Amblyrhynchus cristatus to that of Iguana iguana, another Galapagos marine iguana, the mutation does not affect enzyme kinetics, overview
T9A/I283V
site-directed mutagenesis, the mutations switch the nature of the residues from Amblyrhynchus cristatus to those of Iguana iguana, another Galapagos marine iguana, the mutation affects enzyme kinetics decreasing Km for pyruvate and kcat, overview
D241N
site-directed mutagenesis, the mutant hsows higher activity at pH above 5.5 compared to the wild-type enzyme
E60Q
site-directed mutagenesis, the mutant has a similar pH prodile as the wild-type
D241N
-
site-directed mutagenesis, the mutant hsows higher activity at pH above 5.5 compared to the wild-type enzyme
-
E60Q
-
site-directed mutagenesis, the mutant has a similar pH prodile as the wild-type
-
H88X/H226X
substitution of His 88 and 226 of the eLDHA monomer alters the surface charge of equine LDH tetramer, the residues are located in an important region affecting the catalytic kinetics
D38E
-
site-directed mutagenesis, the mutant shows a twofold reduced substrate inhibition by pyruvate compared to the wild-type enzyme
D38R
-
site-directed mutagenesis, the mutant shows a threefold reduced substrate inhibition by pyruvate compared to the wild-type enzyme
F16Q/C81S/N85R
catalytic efficiency is higher than that of wild-type enzyme, utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+
F16Q/I37K/D38S/C81S/N85R
utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+
S100M
-
a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate
I229A
30% decrease in Km value and 2.6fold increase in kcat value for phenylpyruvate
Q88R
17% decrease in Km value and 3fold increase in kcat value for phenylpyruvate
T235G
slight decrease in specific activity towards phenylpyruvate
N197D
-
1.15fold increase in activity, 2.7fold increase in kcat/Km ratio, 2fold increase in production titer for asymmetric synthesis of (S)-2-hydroxybutanoic acid
S163L
-
decrease in substrate inhibition, the Km value for pyruvate is increased substantially and the turnover number is 60% that of wild type
S100M
-
a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate
D8G
no measurable effect on the Km value for pyruvate, increased thermal stability
R157L
additional information
R157L
mutation appears to deregulate activation by fructose 1,6-bisphosphate, leading to constitutive activation of lactate dehydrogenase
R157L
-
mutation appears to deregulate activation by fructose 1,6-bisphosphate, leading to constitutive activation of lactate dehydrogenase
-
additional information
-
construction of an insertion mutant of gene AA02769, inactivation of AA02769 eliminates the ability of the organism to grow on L-lactate, but not on D-glucose
additional information
-
construction of an insertion mutant of gene AA02769, inactivation of AA02769 eliminates the ability of the organism to grow on L-lactate, but not on D-glucose
-
additional information
-
construct an ethanologenic Bacillus subtilis strain, the ldh gene is disrupted in strain WB700 by chromosomal insertion of the Zymomonas mobilis pyruvate decarboxylase gene pdc and the alcohol dehydrogenase II gene adhB under the control of the ldh native promoter leading to production of etahnol and butanediol by the recombinant strain. But cell growth and glucose consumption rates in strain BS35 are reduced by 70 and 65%, respectively, in comparison to the progenitor strain. To eliminate butanediol production, the acetolactate synthase gene alsS is inactivated resulting in BS36, additional expression of transhydrogenase encoded by gene udhA from Escherichia coli allows a partial recovery of the cell growth rate and an early onset of ethanol production resulting in strain BS37, overview
additional information
-
construct an ethanologenic Bacillus subtilis strain, the ldh gene is disrupted in strain WB700 by chromosomal insertion of the Zymomonas mobilis pyruvate decarboxylase gene pdc and the alcohol dehydrogenase II gene adhB under the control of the ldh native promoter leading to production of etahnol and butanediol by the recombinant strain. But cell growth and glucose consumption rates in strain BS35 are reduced by 70 and 65%, respectively, in comparison to the progenitor strain. To eliminate butanediol production, the acetolactate synthase gene alsS is inactivated resulting in BS36, additional expression of transhydrogenase encoded by gene udhA from Escherichia coli allows a partial recovery of the cell growth rate and an early onset of ethanol production resulting in strain BS37, overview
-
additional information
-
transposon mutagenesis of a reporter strain carrying a chromosomal ldhA promoter-lacZ fusion, PldhA-lacZ, using Tn5-based minitransposon system reveals that ldhA disruption drastically decreases expression of PldhA-lacZ. ldhA Promoter activity is reduced in the ldhA mutant. PldhA-lacZ expression in the ldhA mutant is restored by deletion of lldR, suggesting that LldR acts as a repressor of ldhA in the absence of L-lactate and the LldR-mediated repression is not relieved in the ldhA mutant due to its inability to produce L-lactate. lldR deletion does not affect PldhA-lacZ expression in the wild-type background during growth on either glucose, acetate, or L-lactate. However, it upregulates PldhA-lacZ expression in the sugR mutant background during growth on acetate. The binding sites of LldR and SugR are located around the -35 and -10 regions of the ldhA promoter, respectively
additional information
-
construction of ldh1 and ldh-2 deletion mutants and of a catalytically inactive double knockout mutant of genes ldh-1 and ldh-2 by gene replacement achieved by double-crossover homologous recombination. The ldh-2 mutant shows hardly any differences in growth and metabolism in comparison to the wild-type. The two mutants lacking ldh-1, on the other hand, produce much less lactate than the wild-type but grew to higher cell densities and have higher final pHs, phenotypes, overview
additional information
deletion of Glu 14 of the eLDHB monomer alters the surface charge of equine LDH tetramers and the residue is located in an important region affecting the catalytic kinetics
additional information
deletion of Glu 14 of the eLDHB monomer alters the surface charge of equine LDH tetramers and the residue is located in an important region affecting the catalytic kinetics
additional information
-
deletion of Glu 14 of the eLDHB monomer alters the surface charge of equine LDH tetramers and the residue is located in an important region affecting the catalytic kinetics
additional information
-
the malate dehydrogenase, EC 1.1.1.37, mutant I12V/R81Q/M85E/G210A/V214I shows a substrate specificity that is switched from malate dehydrogenase to that of lactate dehydrogenase, overview
additional information
-
a mutant into which an additional loop has been engineered in order to prevent tetramerization
additional information
the malate dehydrogenase, EC 1.1.1.37, mutant I12V/R81Q/M85E/G210A/V214I shows a substrate specificity that is switched from malate dehydrogenase to that of lactate dehydrogenase, overview
additional information
silencing of LDHB with a small interfering RNA (siRNA) (siLDHB-2) decreasing cell number in all the cancer cell lines investigated
additional information
-
construction of a Pichia stipitis strain CBS6054, that expresses the LDH from Lactobacillus helveticus under the control of the Pichia stipitis fermentative ADH1 promoter, the mutant yeast uses xylose, glucose, or a mixture of the two sugars as the carbon source for lactate production, LDH competes efficiently with the ethanol pathway for pyruvate, overview
additional information
construction of an ldh gene insertion mutant strain FI9078, the insertion of an IS905-like element, that created a hybrid promoter in the intergenic region upstream of ldhB, leads to activation of a second isozyme LDHB, which shows a strongly pH-dependent activity, overview
additional information
-
construction of an ldh gene insertion mutant strain FI9078, the insertion of an IS905-like element, that created a hybrid promoter in the intergenic region upstream of ldhB, leads to activation of a second isozyme LDHB, which shows a strongly pH-dependent activity, overview
additional information
-
construction of an ldh gene insertion mutant strain FI9078, the insertion of an IS905-like element, that created a hybrid promoter in the intergenic region upstream of ldhB, leads to activation of a second isozyme LDHB, which shows a strongly pH-dependent activity, overview
-
additional information
-
N-terminal deletion mutants lacking the first 5 and 10 amino acids of the N-terminus are more sensitive to denaturing environment than wild-type enzyme. They are easily inactivated and unfolded. Their instability increases and their ability to refold decreases with the increased number of amino acid residues removed from the N-terminus of LDH
additional information
-
enhanced stability of L-lactate dehydrogenase through immobilization engineering, the enzyme is immobilized on glyoxyl-agarose, method optimization: preparation of an active and highly stable immobilizedderivative of LDH. with 90.1% immobilization and 72.0% yield is achieved using 300 mM trehalose during the immobilization process. Thermal stabilization factors attained for the immobilized LDH are 1600times greater as compared to its soluble counterpart. The immobilized preparation is also stabilized against ethanol where it recovers 75% of its initial activity after 48 h while the soluble enzyme is completely inactivated after only 10 min under the same conditions. Production of L-lactic acid is achieved in a batch reactor with the immobilized LDH and this preparation resists 15 reuses without the loss of activity. Co-immobilization of LDH and formate dehydrogenase. Immobilization has a negligible effect on the catalytic performance of L-LDH while having a significant impact on its stability
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8 - 7
-
1 h, 25°C, pH 3.8: 50% loss of activity, pH 7.0: stable, mutant enzyme with a deletion of 10 N-terminal amino acids
4 - 8
-
rather stable from pH 4.0 to pH 8.0, but rapid decline in activity below pH 4.0 and above pH 8.0
5.5 - 7
-
1 h, 25°C, pH 5.5: 50% loss of activity, pH 7.0: stable, wilde-type enzyme
5.7 - 7
-
1 h, 25°C, pH 5.7: 50% loss of activity, pH 7.0: stable, mutant enzyme with a deletion of 5 N-terminal amino acids
5.8 - 8.2
purified recombinant enzyme, 1-5 h, 70°C, completely stable
additional information
incubation of TeLdhL at lower pH results in a rapid inactivation of the enzyme
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
46
-
1 h, 25°C, 50% loss of activity, mutant enzyme with a deletion of 10 N-terminal amino acids
5 - 35
50
53
-
20 min, complete loss of activity of isoenzyme A4, about 40% loss of activity of isoenzyme A2B2
55
58
60
65
68
69
70
71
90
additional information
45
inactivation above, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments
50
-
20 min, about 40% loss of activity of isoenzyme A4, about 10% loss of activity of isoenzyme B4, about 25% loss of activity of isoenzyme A2B2
50
purified recombinant enzyme, half-time for inactivation is about 4 h and no residual activity is determined after 9 h, rapid loss of activity above
50
-
1 h, 25°C, 50% loss of activity, mutant enzyme with a deletion of 5 N-terminal amino acids
50
-
2 min, 6% loss of activity in presence of fructose 1,6-diphosphate, NADH and pyruvate, complete loss of activity without protectant
55
-
20 min, about 90% loss of activity of isoenzyme A2B2, about 15% loss of activity of isoenzyme B4
58
-
30 min, stable up to A hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH is named S100M
58
-
30 min, stable up to A hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH is named S100M
60
stable up to, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments
60
-
5 min, complete inactivation without stabilizer, Mn2+ in combination with fructose 1,6-diphosphate stabilizes the enzyme completely
65
-
enzyme activity and electrophoretic pattern of LDH-A4 and malate dehydrogenase, EC 1.1.1.37, compared in relation to heat and urea inactivation, MDH is more sensitive than LDH, overview
70
purified recombinant enzyme, 1-5 h, pH 5.8-8.2, completely stable
90
stable up to, thermal stability in relation to enzyme structure comparison to enzymes from other species in extreme environments
additional information
-
very stable at room temperature, 4°C and 50°C
additional information
-
the enzyme from aerobic control muscle has a significantly higher melting temperature (greater thermal stability) compared to the anoxic enzyme form, suggesting that there is a structural difference between the two enzyme forms. Both anoxic and control LDH are most thermally stable around pH 7.6 although the difference in TM between pH 7.3 and pH 7.6 is not significant for the anoxic LDH
additional information
-
a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate
additional information
-
protection against heat inactivation by 1 mM fructose 1,6-diphosphate, 1 mM ATP, 1 mM glucose 6-phosphate and increased levels of phosphate
additional information
-
a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
fructose-1,6-diphosphate is necessary to stabilize the tetrameric enzyme form
-
irreversible loss of activity after several hours when the concentration is below 0.1 mg protein per ml
-
Mn2+ and fructose 1,6-diphosphate are required during dialysis at pH 5.5, very unstable during dialysis at pH 7.5 although Mn2+ and fructose 1,6-diphosphate are added
-
modification by o-phthalaldehyde not only results in inactivation of the enzyme, but also leads to the enzymes dissociation and partial unfolding
-
N-terminal deletion mutants lacking the first 5 and 10 amino acids of the N-terminus are more sensitive to denaturing environment than wild-type enzyme. They are easily inactivated and unfolded. Their instability increases and their ability to refold decreases with the increased number of amino acid residues removed from the N-terminus of LDH
-
NADH and fructose 1,6-diphosphate partially stabilize the 140000 Da molecular weight form against dissociation in triethanolamine-hydrochloride buffer at pH 8.0
-
the transition midpoints, 50% activity after 1 h incubation in guanidine HCl, are 0.77 M for the mutant enzyme with a deletion of 10 N-terminal amino acids, 0.92 M for the mutant with a deletion of 5 N-terminal amino acids and 1.7 M for the wild-type enzyme
-
very stable during 70 h dialysis in acetate buffer pH 5.5, in imidazol buffer, pH 6.5, in phosphate buffer pH 6.5 with dithioerythritol and in Tris-HCl buffer pH 7.5 with Mn2+ and fructose 1,6-diphosphate
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
-
the immobilized enzyme is also stabilized against ethanol where it recovers 75% of its initial activity after 48 h while the soluble enzyme is completely inactivated after only 10 min under the same conditions
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM sodium phosphate buffer, pH 7.0, stable for several months
-
-5°C, precipitated from phosphate buffer with (NH4)2SO4 and storage in the supernatant solution, stable for several weeks
-
4C, glycerol and DDT containing buffer
stabilized for storage at 4°C by addition of 0.2-1 M potassium chloride or 3.2 M ammonium sulfate
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isozymes LDHB and LDH 400fold and 30fold, from cell extracts of strains FI9078 and MG1363, respectively
native enzyme 34.3fold to about 98% purity by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
-
native enzyme by ultracentrifugation, hydrophobic interaction chromatography, gel filtration, and ultrafiltration
native enzyme from malignant and healthy breast tissue 14.3fold by anion exchange and affinity chromatography
native enzyme to homogeneity from tail muscle of both aerobic control and anoxic crayfish 26.5fold and 69.4fold, respectively, by anion exchange chromatography and two steps of affinity chromatography
-
native enzyme, and recombinant His6-tagged enzyme by nickel affinity chromatography from Escherichia coli BL21(DE3)
-
on cobalt affinity resin
optimization of a molecular analysis method based on the three-dimensional structure of protein and protein-ligand interactions using dye-ligand density for target protein separation, 3.7fold purification with expanded bed affinity adsorption, overview
-
partial
recombinant C-terminally His-tagged enzyme from Escherichia coli strain M15 by nickel affinity chromatography
-
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(lambdaDE3) by centrfugation at 40000 g, nickel affinity chromatography, dialysis and ultrafiltration, followed by gel filtration, to over 95% purity
recombinant enzyme from Escherichia coli strain DH5alpha by heat treatment at 55°C for 90 s, hydrophobic interaction chromatography, hydroxyapatite chromatography, gel filtration, and ultrafiltration
recombinant enzyme from Escherichia coli strain DH5alpha by heat treatment at 70°C for 90 s, anion exchange chromatography, gel filtration, and ultrafiltration
recombinant enzyme from Escherichia coli strain Rosetta (DE3)pLysS by ammonium sulfate fractionation, gel filtration, anion exchange chromatography, and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography to homogeneity
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity and anion exchange chromatography
-
recombinant His6-tagged enzyme from Escherichia coli BL21(DE3) by metal affinity chromatography dialysis, and ultrafiltration
recombinant His6-tagged LdhB from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography and cleavage of the tag
-
recombinant N-termially His6-tagged LDH-1 from Escherichia coli BL21 by nickel affinity chromatography and gel filtration to homogeneity
-
recombinant wild-type and mutant enzymes from Escherichia coli strain JM109 by ion-exchange chromatography and affinity chromatography, respectively
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a chimeric bifunctional enzyme composing of galactose dehydrogenase from Pseudomonas fluorescens and lactate dehydrogenase from Bacillus stearothermophilus is successfully constructed and expressed in Escherichia coli
-
development of a recombinant yeast exhibiting efficient lactate production by substituting the coding region of PDC1 on chromosome XII for that of LDH through homologous recombination
expressed in Leuconostoc citreum using a shuttle vector pLeuCM, change of the pyruvate carbon flux in Leuconostoc citreum from D-lactate into L-lactate by heterologous expression of L-lactate dehydrogenase
expressed in Saccharomyces cerevisiae replacing disrupted pyruvate decarboxylase 1 and alcohol dehydrogenase 1
-
expression in Escherichia coli
expression in Escherichia coli as maltose-binding protein fusion protein. CpLDH1 is probably evolved from the same ancestor of CpMalDH1 by a very recent gene duplication that occurs after Cryptosporidium parvum diverges from other apocomplexans
expression in Escherichia coli HB101 using a pEMBL vector. The gene is strongly expressed in the vector used if the orientation of the insert allows the LDH promoter and the vector's lac promoter to direct transcription in the same direction
expression in Escherichia coli strain DH5alpha
expression in Pichia stipidis strain CBS6054, subcloning in Escherichia coli strain DH5alpha
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
-
expression of wild-type and mutant enzymes in Escherichia coli strain JM109
-
gene AA02769 or lctD, DNA and amino acid sequence determination and analysis, subcloning in Escherichia coli DH5alpha, expression as His6-tagged protein in Escherichia coli BL21(DE3)
-
gene ldh, real-time quantitative reverse transcription-PCR enzyme expression analysis
gene ldh, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain M15
-
gene ldh-1, DNA and amino acid sequence determinaation and analysis, sequence comparisons, recombinant expression in Escherichia coli
gene ldh-1, expression of N-termially His6-tagged enzyme in Escherichia coli BL21
-
gene ldh-2, DNA and amino acid sequence determinaation and analysis, sequence comparisons, recombinant expression in Escherichia coli
gene ldh-a, DNA and amino acid sequence determination and analysis
gene LDH1, recombinant expression of the enzyme in Escherichia coli strain Rosetta (DE3)pLysS, molecular replacement and modelling using the structure of PfLDH, PDB ID 1T2D
gene ldhB, from strain NRRL 395 and 99-880, expression of His6-tagged LdhB in Escherichia coli strain BL21(DE3)
-
gene ldhL, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli
gene ldhL, DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme in Escherichia coli BL21(DE3)
gene pfldh, recombinant expression in Saccharomyces cerevisiae, the optimized engineered strain is used as host for L-lactic acid fermentation. Strain IBB10B05 incorporates a NADH-dependent pathway for oxidoreductive xylose assimilation within CEN.PK113-7D background and is additionally evolved for accelerated xylose-to-ethanol fermentation. The pfldh gene is placed in strain IBB10B05 at the pdc1 locus under control of the pdc1 promotor, and strain IBB14LA1_5 additionally has the pdc5 gene disrupted resulting in strain IBB14LA1. The Saccharomyces cerevisiae strain originally optimized for xylose-to-ethanol fermentation is useful to implement L-lactic acid production from glucose and xylose
genes ldh and ldhB, sequence determination, analysis, and comparison
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
into expression plasmid pTUB8Myc-His-X-HX under the control of a modified tubulin promoter. Type I strain of Toxoplasma gondii RHDELTAHX transformed with plasmid. Transgenic parasites overexpressing LDH1
into expression plasmid pTUB8Myc-His-X-HX under the control of a modified tubulin promoter. Type I strain of Toxoplasma gondii RHDELTAHX transformed with plasmid. Transgenic parasites overexpressing LDH2
into pET-SUMO and expressed as 6 His Tag in Escherichia coli BL21
into plasmid pET-30a and expressed with a His tag in Escherichia coli BL21/DE3
-
into pQE-30 Xa vector and expressed in Escherichia coli SG13009 cells
-
LDHA, DNA and amino acid sequence determination and analysis, genetic structure, and sequence comparisons, phylogenetic analysis, overview
LDHB, DNA and amino acid sequence determination and analysis, genetic structure, and sequence comparisons, phylogenetic analysis, overview
multiple initiation sites required for transcription of the LDHA gene are identified in its promoter region, including a cAMP response element (CRE) and E-box motif. The LDHA gene promoter possesses also two conserved hypoxia response elements (HREs) containing functionally essential binding sites for hypoxia-inducible factor 1 (HIF-1) with the consensus sequence 5?-RCGTG-3?, which may strongly suggest an oxygendependent regulation of LDH-5 activity
N-terminal deletion mutants lacking the first 5 and 10 amino acids of the N-terminus are expressed in Escherichia coli
-
recombinant expression of C-terminally His6-tagged enzyme from pET-29b-LDHA vector in Escherichia coli strain BL21(lambdaDE3)
development of a recombinant yeast exhibiting efficient lactate production by substituting the coding region of PDC1 on chromosome XII for that of LDH through homologous recombination
development of a recombinant yeast exhibiting efficient lactate production by substituting the coding region of PDC1 on chromosome XII for that of LDH through homologous recombination
-
expression in Escherichia coli HB101 using a pEMBL vector. The gene is strongly expressed in the vector used if the orientation of the insert allows the LDH promoter and the vector's lac promoter to direct transcription in the same direction
-
expression in Escherichia coli HB101 using a pEMBL vector. The gene is strongly expressed in the vector used if the orientation of the insert allows the LDH promoter and the vector's lac promoter to direct transcription in the same direction
-
gene ldh-a, DNA and amino acid sequence determination and analysis
into pET-SUMO and expressed as 6 His Tag in Escherichia coli BL21
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
deletion of water-forming NADH oxidase NOX in Streptococcus mutans leads to significantly elevated lactate dehydrogenase activity and gene ldh transcription in the DELTAnox strain, which is mediated in part by the redox-sensing regulator Rex. Rex activation of ldh transcription
expression of LutACB is induced by iron-limited conditions
in the absence of sugar, SugR binds to the ldhA promoter region, thereby repressing ldhA expression. LldR also binds to the ldhA promoter region, thus negatively regulating ldhA expression. LldR is an L-lactate-responsive transcriptional repressor of L-lactate utilization genes
-
L-leucine depletion decreases the proteins synthesis, and also decreases L-lactate dehydrogenase B chain mRNA expression in bovine mammary alveolar cells cells
Spatholobus suberectus extract has a strong inhibitory effect on LDH-5 expression and activity inboth estrogen-dependent and estrogen-independent human breast cancer cells. Follicle-stimulating hormone, insulin, insulin-like growth factor 1, epidermal growth factor, and tumor necrosis factor alpha, are factors able to affect LDHA gene transcription through relevant intracellular signal transduction systems, including protein kinase A and C signaling pathways
the enzyme is induced at 37°C by 0.5 mM beta-D-thiogalactoside concentration being associated with inclusion bodies. By reducing cell growth temperature to 15°C and sopropyl beta-D-thiogalactoside concentration to 0.25 mM, it is possible to get approximately 82% of expressed protein in soluble form
-
deletion of water-forming NADH oxidase NOX in Streptococcus mutans leads to significantly elevated lactate dehydrogenase activity and gene ldh transcription in the DELTAnox strain, which is mediated in part by the redox-sensing regulator Rex. Rex activation of ldh transcription
deletion of water-forming NADH oxidase NOX in Streptococcus mutans leads to significantly elevated lactate dehydrogenase activity and gene ldh transcription in the DELTAnox strain, which is mediated in part by the redox-sensing regulator Rex. Rex activation of ldh transcription
-
-
expression of LutACB is induced by iron-limited conditions
Q5F885; Q5F884; Q5F883
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
denaturation in 6 M guanudine HCl for 2 min, then dilution 100fold in 0.1 M phosphate buffer, pH 7.5, containing 10 mM beta-mercaptoethanol. After standing for 1 h 18% of the wild-type activity is regained, 20% is regained after 12 h. The mutant enzyme with a deletion of 5 N-terminal amino acids is restored to 15% and 17% after 1 h and 12 h renaturation. The mutant with a deletion of 10 N-terminal amino acids can only be restored to 3% of the original activity after 1 h renaturation and at most 7% after 12 h
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
L-leucine depletion decreases the proteins synthesis, and also decreases L-lactate dehydrogenase B chain mRNA expression in bovine mammary alveolar cells
analysis
biotechnology
degradation
diagnostics
drug development
medicine
synthesis
analysis
CpLDH with APAD+ may be useful as a diagnostic tool for detection of protozoan parasite Cryptosporidium
analysis
construction of multiplexed direct electron transfer-type lactate and glucose sensors using a fusion enzyme between L-lactate oxidase from Aerococcus viridans, A96L/N212K mutant, which is minimized in its oxidase activity and b-type cytochrome protein. The sensors achieve simultaneous detection of lactate and glucose without cross-talking error, with the detected linear ranges of 0.5-20 mM for lactate and 0.1-5 mM for glucose, sensitivities of 4.1 nA/mM x mm2 for lactate and 56 nA/mM x mm2 for glucose, and limit of detections of 0.41 mM for lactate and 0.057 mM for glucose
analysis
-
reproducible and validated LDH assay optimized for several cell types for application in clinical medicine and biomedical sciences. Assay is cost effective and allows for experiment-specific optimization
biotechnology
-
a chimeric bifunctional enzyme composing of galactose dehydrogenase from Pseudomonas fluorescens and lactate dehydrogenase from Bacillus stearothermophilus is successfully constructed. The chimeric enzyme is able to recycle NAD with a continuous production of lactate without any externally added NADH
biotechnology
-
genetic tools for use in Clostridium thermocellum that allow creation of unmarked mutations while using a replicating plasmid. The strategy employs counter-selections developed from the native C. thermocellum hpt gene and the Thermoanaerobacterium saccharolyticum tdk gene and is used to delete the genes for both lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta)
biotechnology
Acetivibrio thermocellus DSM 1237
-
genetic tools for use in Clostridium thermocellum that allow creation of unmarked mutations while using a replicating plasmid. The strategy employs counter-selections developed from the native C. thermocellum hpt gene and the Thermoanaerobacterium saccharolyticum tdk gene and is used to delete the genes for both lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta)
-
degradation
direct conversion of switchgrass to ethanol without conventional pretreatment of the biomass is accomplished by deletion of lactate dehydrogenase and heterologous expression of a Clostridium thermocellum bifunctional acetaldehyde/alcohol dehydrogenase. Whereas wild-type Caldicellulosiruptor bescii lacks the ability to make ethanol, 70% of the fermentation products in the engineered strain are ethanol (12.8 mM ethanol directly from 2% wt/vol switchgrass) with decreased production of acetate by 38% compared with wild-type
degradation
-
direct conversion of switchgrass to ethanol without conventional pretreatment of the biomass is accomplished by deletion of lactate dehydrogenase and heterologous expression of a Clostridium thermocellum bifunctional acetaldehyde/alcohol dehydrogenase. Whereas wild-type Caldicellulosiruptor bescii lacks the ability to make ethanol, 70% of the fermentation products in the engineered strain are ethanol (12.8 mM ethanol directly from 2% wt/vol switchgrass) with decreased production of acetate by 38% compared with wild-type
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diagnostics
low LDH affinity kinetics can be a diagnostic parameter for human breast cancer
diagnostics
LDH levels might serve as a significant prognostic factor in high-risk patients with metastatic renal cell carcinoma (RCC) and a predictive factor associated with the response and survival benefit of the mTOR complex-1 (mTORC1) inhibitor temsirolimus. LDH is one of the risk factors included in the international prognostic index (IPI) and it is considered a strong predictor of survival of patients with aggressive lymphoid cancers. Serum LDH level inversely correlates with the survival of patients with small cell lung cancer (SCLC) and allows the selection of very high-risk patients. Serum LDH might be a useful marker for predicting global clinical outcomes in hepatocellular carcinoma patients treated with a tyrosine kinase inhibitor (sorafenib). The determination of serum LDH levels appears to be a helpful clinical tool also in the diagnosis of prostate cancer and in the control of androgenic treatment
drug development
-
parasite LDH is a target for antimalarial compounds owing to structural and functional differences from the human isozymes
drug development
-
a selective lactate dehydrogenase inhibitor targeting the L-malate dehydrogenase function of Plasmodium falciparum and its corresponding tricarboxylic acid cycle provides an attractive therapeutic opportunity, in contrast to LDH targeting due to the functional similarity between human and parasite LDHs
drug development
-
LDH is critically implicated in tumor growth and therefore considered to be an important target protein for antitumor metal complexes
drug development
-
LDH is a potential drug target and candidate antigen for immunodiagnosis (LDH can be recognized in serum from swine or patient infected with Taenia asiatica) and vaccine for taeniasis and viscero-cysticercosis caused by Taenia asiatica
drug development
-
Sa-LDH-1 can become a potential drug target for antibiotics against Staphylococcus aureus
drug development
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the parasite enzyme is a potential target for antimalarial drugs
drug development
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LDH is critically implicated in tumor growth and therefore considered to be an important target protein for antitumor metal complexes
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medicine
suitable drug target for design of novel babesial chemotherapeutics
medicine
structural characterization of the enzyme and active-site differences from the human lactate dehydrogenase may be useful for structural-based design of new treatments for toxoplasmic infections
medicine
-
serum LDH zymograms of patients can be used as prognostic marker, since they tend to reach the normal level during recovery signifying the effect of chemotherapy in hospitalized patients. Elevation along with the rise in total LDH activity may be used in the diagnosis and monitoring of tubercular pyothorax
medicine
LDH-5 is considered a highly promising target in cancer therapy, LDH-5 significance in the treatment and prognosis of neoplastic diseases
medicine
-
alpha-HBDH is an independent risk factor for systemic lupus erythematosus-related liver injury. alpha-HBDH level is significantly higher in the systemic lupus erythematosus-related liver injury patients than in the non-systemic lupus erythematosus-related liver injury patients. alpha-HBDH is positively correlated with levels of aspartate aminotransferase and lactate dehydrogenase, the aspartate aminotransferase/alanine aminotransferase ratio, and the systemic lupus erythematosus disease activity index 2000, and it is negatively correlated with albumin and C3. The optimal cutoff value of alpha-HBDH for distinguishing systemic lupus erythematosus patients with and without liver injury is 258.50 U/l, which provides a 60.94% sensitivity and a 94.67% specificity
medicine
-
HBDH is associated with atherothrombotic events in 83 stable patients undergoing infrainguinal angioplasty and stenting. HBDH levels at baseline are significantly higher in patients who subsequently developed the primary endpoint. HBDH can distinguish between patients without and with future atherothrombotic events. A HBDH concentration at/above 115 U/l is the best threshold to predict the composite endpoint, providing a sensitivity of 83.3% and a specificity of 71.4%, and is therefore defined as high HBDH. Ischemic events occur significantly more often in patients with high HBDH than in patients with lower HBDH levels
medicine
-
alpha-hydroxybutyrate dehydrogenase as an independent prognostic factor for mortality in hospitalized patients with COVID-19. Among 1751 patients with confirmed COVID-19, 15 patients (0.87%) died. The mortality during hospitalization was 0.26% for patients with normal alpha-HBDH levels and 5.73% for those with elevated alpha-HBDH levels
synthesis
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the enzyme has a commercial significance, as it can be used to produce chiral building blocks for the synthesis of key pharmaceuticals and agrochemicals, optimization of enzyme reaction by engineering to eliminate the substrate inhibition
synthesis
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development of yeast-based bioprocesses to produce lactate from lignocellulosic raw material
synthesis
construction of a markerless strain lacking phosphotransacetylase Pta, acetate kinase Ack and lactate dehydrogenase Ldh genes. The gene deletion strain ferments 50 g/liter of cellobiose, with a yield of 0.44 g ethanol per g glucose equivalent substrate and a maximum volumetric productivity of 1.13 g ethanol per liter and h. A system for genetic marker removal allows for enactment of further modifications and creation of strains for industrial applications
synthesis
-
Thermoanaerobacter mathranii can produce ethanol from lignocellulosic biomass at high temperatures. Deletion of the Ldh gene coding for lactate dehydrogenase eliminates an NADH oxidation pathway. To further facilitate NADH regeneration used for ethanol formation, a heterologous gene GldA encoding an NAD+-dependent glycerol dehydrogenase is expressed leading to increased ethanol yield in the presence of glycerol using xylose as a substrate. The metabolism of the cells is shifted toward the production of ethanol over acetate, hence restoring the redox balance. The recombinant enzyme acquired the capability to utilize glycerol as an extra carbon source in the presence of xylose resulting in a higher ethanol yield
synthesis
-
metabolic engineering of Geobacillus thermoglucosidasius to divert the fermentative carbon flux from a mixed acid pathway, to one in which ethanol becomes the major product, involving elimination of the lactate dehydrogenase and pyruvate formate lyase pathways by disruption of the ldh and pflB genes, respectively, and upregulation of expression of pyruvate dehydrogenase. Strains with all three modifications form ethanol efficiently and rapidly at temperatures in excess of 60°C in yields in excess of 90% of theoretical. The strains also efficiently ferment cellobiose and a mixed hexose and pentose feed
synthesis
-
a lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta) deletion strain is evolved for 2,000 h, resulting in a stable strain with 40:1 ethanol selectivity and a 4.2-fold increase in ethanol yield over the wild-type strain. In a coculture of organic acid-deficient engineered strains of both Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, fermentation of 92 g/liter Avicel results in 38 g/liter ethanol, with acetic and lactic acids below detection limits, in 146 h. engineering is based on a phosphoribosyl transferase (Hpt) deletion strain, which produces acetate, lactate, and ethanol in a ratio of 1.7:1.5:1.0, similar to the 2.1:1.9:1.0 ratio produced by the wild type. The Hpt/Ldh double mutant strain does not produce significant levels of lactate and has a 1.4:1.0 ratio of acetate to ethanol. Similarly, the Hpt/Pta double mutant strain does not produce acetate and has a 1.9:1.0 ratio of lactate to ethanol. The Hpt/Ldh/Pta triple mutant strain achieves ethanol selectivity of 40:1 relative to organic acids
synthesis
L-nLDH is an efficient catalyst that can be used in the enantioselective reduction of alpha-keto acids to alpha-hydroxy acids
synthesis
coexpression of enzyme and glucose dehydrogenase gene in Escherichia coli efficiently reduces 3,4-dihydroxyphenylpyruvate to L-3,4-dihydroxyphenyllactate with 95.45% isolation yield
synthesis
engineering of Kluyveromyces marxianus to express and coexpress various heterologous LDH enzymes for L-lactic acid production. LDH enzymes originating from Staphylococcus epidermidis (SeLDH, optimal at pH 5.6), Lactobacillus acidophilus (LaLDH, optimal at pH 5.3), and Bos taurus (BtLDH, optimal at pH 9.8) are functionally expressed individually and in combination. A strain coexpressing SeLDH and LaLDH produces 16.0 g/l L-lactic acid, whereas the strains expressing those enzymes individually produces only 8.4 and 6.8 g/l, respectively. This coexpressing strain produces 24.0 g/l L-lactic acid with a yield of 0.48 g/g glucose in the presence of CaCO3
synthesis
engineering of Kluyveromyces marxianus to express and coexpress various heterologous LDH enzymes for L-lactic acid production. LDH enzymes originating from Staphylococcus epidermidis (SeLDH, optimal at pH 5.6), Lactobacillus acidophilus (LaLDH, optimal at pH 5.3), and Bos taurus (BtLDH, optimal at pH 9.8) are functionally expressed individually and in combination. A strain co-expressing SeLDH and LaLDH produces 16.0 g/l L-lactic acid, whereas the strains expressing those enzymes individually produces only 8.4 and 6.8 g/l, respectively. This coexpressing strain produces 24.0 g/l L-lactic acid with a yield of 0.48 g/g glucose in the presence of CaCO3
synthesis
production of phenyllactic acid from L-Phe by recombinant Escherichia coli coexpressing L-phenylalanine oxidase and L-lactate dehydrogenase. At optimal conditions (L-Phe 6 g/l, pH 7.5, 35°C, CDW 24.5 g/l and 200 rpm), the recombinant strain produces 1.62 g L-phenylalanine/l with a conversion of 28% from L-Phe
synthesis
-
engineering of Kluyveromyces marxianus to express and coexpress various heterologous LDH enzymes for L-lactic acid production. LDH enzymes originating from Staphylococcus epidermidis (SeLDH, optimal at pH 5.6), Lactobacillus acidophilus (LaLDH, optimal at pH 5.3), and Bos taurus (BtLDH, optimal at pH 9.8) are functionally expressed individually and in combination. A strain co-expressing SeLDH and LaLDH produces 16.0 g/l L-lactic acid, whereas the strains expressing those enzymes individually produces only 8.4 and 6.8 g/l, respectively. This coexpressing strain produces 24.0 g/l L-lactic acid with a yield of 0.48 g/g glucose in the presence of CaCO3
-
synthesis
Lactiplantibacillus plantarum ATCC BAA-793
-
production of phenyllactic acid from L-Phe by recombinant Escherichia coli coexpressing L-phenylalanine oxidase and L-lactate dehydrogenase. At optimal conditions (L-Phe 6 g/l, pH 7.5, 35°C, CDW 24.5 g/l and 200 rpm), the recombinant strain produces 1.62 g L-phenylalanine/l with a conversion of 28% from L-Phe
-
synthesis
-
engineering of Kluyveromyces marxianus to express and coexpress various heterologous LDH enzymes for L-lactic acid production. LDH enzymes originating from Staphylococcus epidermidis (SeLDH, optimal at pH 5.6), Lactobacillus acidophilus (LaLDH, optimal at pH 5.3), and Bos taurus (BtLDH, optimal at pH 9.8) are functionally expressed individually and in combination. A strain coexpressing SeLDH and LaLDH produces 16.0 g/l L-lactic acid, whereas the strains expressing those enzymes individually produces only 8.4 and 6.8 g/l, respectively. This coexpressing strain produces 24.0 g/l L-lactic acid with a yield of 0.48 g/g glucose in the presence of CaCO3
-
synthesis
Acetivibrio thermocellus DSM 1237
-
a lactate dehydrogenase (Ldh) and phosphotransacetylase (Pta) deletion strain is evolved for 2,000 h, resulting in a stable strain with 40:1 ethanol selectivity and a 4.2-fold increase in ethanol yield over the wild-type strain. In a coculture of organic acid-deficient engineered strains of both Clostridium thermocellum and Thermoanaerobacterium saccharolyticum, fermentation of 92 g/liter Avicel results in 38 g/liter ethanol, with acetic and lactic acids below detection limits, in 146 h. engineering is based on a phosphoribosyl transferase (Hpt) deletion strain, which produces acetate, lactate, and ethanol in a ratio of 1.7:1.5:1.0, similar to the 2.1:1.9:1.0 ratio produced by the wild type. The Hpt/Ldh double mutant strain does not produce significant levels of lactate and has a 1.4:1.0 ratio of acetate to ethanol. Similarly, the Hpt/Pta double mutant strain does not produce acetate and has a 1.9:1.0 ratio of lactate to ethanol. The Hpt/Ldh/Pta triple mutant strain achieves ethanol selectivity of 40:1 relative to organic acids
-
synthesis
-
Thermoanaerobacter mathranii can produce ethanol from lignocellulosic biomass at high temperatures. Deletion of the Ldh gene coding for lactate dehydrogenase eliminates an NADH oxidation pathway. To further facilitate NADH regeneration used for ethanol formation, a heterologous gene GldA encoding an NAD+-dependent glycerol dehydrogenase is expressed leading to increased ethanol yield in the presence of glycerol using xylose as a substrate. The metabolism of the cells is shifted toward the production of ethanol over acetate, hence restoring the redox balance. The recombinant enzyme acquired the capability to utilize glycerol as an extra carbon source in the presence of xylose resulting in a higher ethanol yield
-
synthesis
-
metabolic engineering of Geobacillus thermoglucosidasius to divert the fermentative carbon flux from a mixed acid pathway, to one in which ethanol becomes the major product, involving elimination of the lactate dehydrogenase and pyruvate formate lyase pathways by disruption of the ldh and pflB genes, respectively, and upregulation of expression of pyruvate dehydrogenase. Strains with all three modifications form ethanol efficiently and rapidly at temperatures in excess of 60°C in yields in excess of 90% of theoretical. The strains also efficiently ferment cellobiose and a mixed hexose and pentose feed
-
synthesis
-
L-nLDH is an efficient catalyst that can be used in the enantioselective reduction of alpha-keto acids to alpha-hydroxy acids
-
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Release 2026.1 (March 2026)
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