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Information on EC 1.1.1.345 - D-2-hydroxyacid dehydrogenase (NAD+)
for references in articles please use BRENDA:EC1.1.1.345
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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
1.1.1.345 D-2-hydroxyacid dehydrogenase (NAD+)
IUBMB Comments
The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+).
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
showSynonyms
d-mandelate dehydrogenase, d-2-hydroxyisocaproate dehydrogenase, d-isomer-specific 2-hydroxyacid dehydrogenase, d-hicdh, mandh2, d-mdh, nad-dependent d-2-hydroxyacid dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-2-hydroxyacid dehydrogenase
D-2-hydroxyisocaproate dehydrogenase
D-HicDH
D-isomer specific 2-hydroxyacid dehydrogenase
D-isomer-specific 2-hydroxyacid dehydrogenase
D-lactate dehydrogenase
D-lactate:NAD+ oxidoreductase
D-malate dehydrogenases
D-mandelate dehydrogenase
D-ManDH1
-
the strain contains at least two distinct forms of D-ManDH, the two apparent D-mandelate dehydrogenases are named D-ManDH1 and D-ManDH2 according to the order of their elution
D-ManDH2
D-MDH
D2-HDH
HdhD
Ldb1010
ldh1837
LEUM_1837
NAD-dependent D-2-hydroxyacid dehydrogenase
PanE
D-isomer specific 2-hydroxyacid dehydrogenase
-
D-isomer specific 2-hydroxyacid dehydrogenase
-
-
D-ManDH2
-
the strain contains at least two distinct forms of D-ManDH, the two apparent D-mandelate dehydrogenases are named D-ManDH1 and D-ManDH2 according to the order of their elution
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an (R)-2-hydroxycarboxylate + NAD+ = a 2-oxocarboxylate + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
L-leucine degradation IV (reductive Stickland reaction)
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SYSTEMATIC NAME
IUBMB Comments
(R)-2-hydroxycarboxylate:NAD+ oxidoreductase
The enzymes, characterized from bacteria (Peptoclostridium difficile, Enterococcus faecalis and from lactic acid bacteria) prefer substrates with a main chain of 5 carbons (such as 4-methyl-2-oxopentanoate) to those with a shorter chain. It also utilizes phenylpyruvate. The enzyme from the halophilic archaeon Haloferax mediterranei prefers substrates with a main chain of 3-4 carbons (pyruvate and 2-oxobutanoate). cf. EC 1.1.1.272, (D)-2-hydroxyacid dehydrogenase (NADP+).
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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
(R)-2-hydroxy-4-methylpentanoate + NAD+
4-methyl-2-oxopentanoate + NADH + H+
-
Substrates: i.e. (R)-2-hydroxyisocaproate
Products: i.e. 2-oxoisocaproate
Products: i.e. 2-oxoisocaproate
r
2-hydroxyhexanoate + NAD+
2-oxohexanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
2-hydroxyoctanoate + NAD+
2-oxooctanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
2-hydroxypentanoate + NAD+
2-oxopentanoate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
2-oxomethylthiobutyrate + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxooctanoate + NADH + H+
2-hydroxyoctanoate + NAD+
-
Substrates: -
Products: -
Products: -
r
3-(4-hydroxyphenyl)-2-oxopropanoate + NADH + H+
2-hydroxy-3-(4-hydroxyphenyl)propanoate + NAD+
-
Substrates: -
Products: -
Products: -
?
4-methyl-2-oxopentanoate + NADH + H+
4-methyl-2-hydroxypentanoate + NAD+
-
Substrates: highest Vmax/Km value of all substrates tested
Products: -
Products: -
?
D-2-hydroxybutyrate + NAD+
2-oxobutyrate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
DL-2-hydroxyisocaproate + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
r
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Substrates: Vmax/Km is 1% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Substrates: Vmax/KM is less than 1% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
(R)-mandelate + NAD+
phenylglyoxylate + NADH + H+
-
Substrates: Vmax/Km is 0.4% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-formylbutanethioate + NADH + H+
?
-
Substrates: i.e. 2-ketomethylthiobutyrate
Products: -
Products: -
?
2-formylbutanethioate + NADH + H+
?
Lactococcus cremoris TIL46
-
Substrates: i.e. 2-ketomethylthiobutyrate
Products: -
Products: -
?
2-oxo-3-phenylpropanoate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: Vmax/Km is 2.7% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxo-3-phenylpropanoate + NADH + H+
2-hydroxy-3-phenylpropanoate + NAD+
-
Substrates: Vmax/KM is 1.9% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
Substrates: Vmax/Km is 0.25% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxobutanoate + NADH + H+
2-hydroxybutanoate + NAD+
-
Substrates: Vmax/KM is less than 1% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
2-hydroxybutyrate + NAD+
Substrates: -
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
D-2-hydroxybutyrate + NAD+
-
Substrates: 55% activity compared to pyruvate
Products: -
Products: -
r
2-oxobutyrate + NADH + H+
D-2-hydroxybutyrate + NAD+
-
Substrates: 55% activity compared to pyruvate
Products: -
Products: -
r
2-oxocarboxylate + NADH + H+
(R)-2-hydroxycarboxylate + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxocarboxylate + NADH + H+
(R)-2-hydroxycarboxylate + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Substrates: Vmax/Km is 5.1% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Substrates: Vmax/KM is 3% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Substrates: Vmax/Km is 4.1% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
-
Substrates: i.e. 2-oxovalerate
Products: -
Products: -
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
Substrates: i.e. 2-oxocaproate
Products: -
Products: -
r
2-oxohexanoate + NADH + H+
2-hydroxyhexanoate + NAD+
Substrates: i.e. 2-oxocaproate
Products: -
Products: -
?
2-oxoisocaproate + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxoisocaproate + NADH + H+
L-2-hydroxyisocaproate + NAD+
-
Substrates: 29% activity compared to pyruvate
Products: -
Products: -
r
2-oxoisocaproate + NADH + H+
L-2-hydroxyisocaproate + NAD+
-
Substrates: 29% activity compared to pyruvate
Products: -
Products: -
r
2-oxoisovalerate + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxomethylvalerate + NADH + H+
? + NAD+
-
Substrates: -
Products: -
Products: -
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Substrates: Vmax/Km is 7.6% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Substrates: Vmax/KM is 10.6% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Substrates: Vmax/Km is 5.8% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
-
Substrates: i.e. 2-oxocaproate
Products: -
Products: -
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
Substrates: i.e. 2-oxovalerate
Products: -
Products: -
r
2-oxopentanoate + NADH + H+
2-hydroxypentanoate + NAD+
Substrates: i.e. 2-oxovalerate
Products: -
Products: -
?
3-hydroxypyruvate + NADH + H+
?
Lactiplantibacillus plantarum ATCC 8041
-
Substrates: -
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
-
Substrates: i.e.2-oxoisovalerate
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH + H+
2-hydroxy-3-methylbutanoate + NAD+
Lactococcus cremoris TIL46
-
Substrates: i.e.2-oxoisovalerate
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Substrates: Vmax/Km is 51% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Substrates: Vmax/KM is 56% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
3-methyl-2-oxobutanoate + NADH + H+
3-methyl-2-hydroxybutanoate + NAD+
-
Substrates: Vmax/Km is 85.7% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
3-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-3-methylpentanoate + NAD+
-
Substrates: i.e. 2-oxomethylvalerate
Products: -
Products: -
?
3-methyl-2-oxopentanoate + NADH + H+
2-hydroxy-3-methylpentanoate + NAD+
Lactococcus cremoris TIL46
-
Substrates: i.e. 2-oxomethylvalerate
Products: -
Products: -
?
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
Substrates: i.e. 2-oxoisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
Substrates: i.e. 2-oxoisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
Substrates: i.e. 2-oxoisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
?
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
-
Substrates: i.e. 2-oxoisocaproate. The apparent Vmax/Km ratio for the reverse reaction is about 0.5% of that for the forward reaction
Products: i.e. (R)-2-hydroxyisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
r
4-methyl-2-oxopentanoate + NADH + H+
(R)-2-hydroxy-4-methylpentanoate + NAD+
Lactococcus cremoris TIL46
-
Substrates: i.e. 2-oxoisocaproate. The apparent Vmax/Km ratio for the reverse reaction is about 0.5% of that for the forward reaction
Products: i.e. (R)-2-hydroxyisocaproate
Products: i.e. (R)-2-hydroxyisocaproate
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
L-2-hydroxycaproate + NAD+
2-oxocaproate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
L-2-hydroxycaproate + NAD+
2-oxocaproate + NADH + H+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADH + H+
D-malate + NAD+
Substrates: -
Products: -
Products: -
r
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Substrates: Vmax/Km is 44% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Substrates: Vmax/KM is 54% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
phenylglyoxylate + NADH + H+
hydroxy(phenyl)acetic acid + NAD+
-
Substrates: Vmax/Km is 16.7% compared to 4-methyl-2-oxopentanoate
Products: -
Products: -
?
phenylpyruvate + NADH + H+
phenyl-D-lactate + NAD+
Substrates: -
Products: -
Products: -
r
phenylpyruvate + NADH + H+
phenyl-D-lactate + NAD+
Substrates: -
Products: -
Products: -
r
phenylpyruvate + NADH + H+
phenyllactate + NAD+
-
Substrates: -
Products: -
Products: -
?
phenylpyruvate + NADH + H+
phenyllactate + NAD+
Substrates: -
Products: -
Products: -
r
phenylpyruvate + NADH + H+
phenyllactate + NAD+
Substrates: -
Products: -
Products: -
?
phenylpyruvate + NADH + H+
phenyllactate + NAD+
-
Substrates: -
Products: -
Products: -
?
phenylpyruvate + NADH + H+
phenyllactate + NAD+
Lactococcus cremoris TIL46
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
D-lactate + NAD+
-
Substrates: 100% activity
Products: -
Products: -
r
pyruvate + NADH + H+
D-lactate + NAD+
-
Substrates: 100% activity
Products: -
Products: -
r
pyruvate + NADH + H+
lactate + NAD+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
lactate + NAD+
Lactiplantibacillus plantarum ATCC 8041
-
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: both enzymes (D-mandelate dehydrogenase D-ManDH1 and D-mandelate dehydrogenase D-ManDH2) exhibit no or very little activity toward small 2-oxoacid substrates, such as pyruvate, hydroxypyruvate, and 2-oxobutyrate, and much higher activity toward substrates with larger aliphatic or aromatic side chains. The two enzymes exhibit higher activity (smaller Km and larger Vmax) for 2-ketoacid substrates branched at the C3 or C4 position than for unbranched substrates; i.e., 2-oxoisovalerate and 2-oxoisocaproate are more favorable than 2-oxovalerate and 2-oxocaproate, respectively. Among aromatic substrates, the two enzymes prefer benzoylformate to phenylpyruvate by 9- and 17-fold, respectively
Products: -
Products: -
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additional information
?
-
-
Substrates: the recombinant enzyme exhibits high catalytic activity toward various 2-oxoacid substrates with bulky hydrophobic side chains, particularly C3-branched substrates such as benzoylformate and 2-oxoisovalerate
Products: -
Products: -
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additional information
?
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Substrates: both enzymes (D-mandelate dehydrogenase D-ManDH1 and D-mandelate dehydrogenase D-ManDH2) exhibit no or very little activity toward small 2-ketoacid substrates, such as pyruvate, hydroxypyruvate, and 2-ketobutyrate, and much higher activity toward substrates with larger aliphatic or aromatic side chains. The two enzymes exhibit higher activity (smaller Km and larger Vmax) for 2-ketoacid substrates branched at the C3 or C4 position than for unbranched substrates; i.e., 2-ketoisovalerate and 2-ketoisocaproate are more favorable than 2-ketovalerate and 2-ketocaproate, respectively. Among aromatic substrates, the two enzymes preferr benzoylformate to phenylpyruvate by 9- and 17-fold, respectively
Products: -
Products: -
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additional information
?
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Substrates: no significant activity with L-lactate, L-2-hydroxybutyrate, L-hydroxyisocaproate, phenylpyruvate, 2-oxomethyl-n-valerate, and 2-oxoisovalerate
Products: -
Products: -
?
additional information
?
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Substrates: no significant activity with L-lactate, L-2-hydroxybutyrate, L-hydroxyisocaproate, phenylpyruvate, 2-oxomethyl-n-valerate, and 2-oxoisovalerate
Products: -
Products: -
?
additional information
?
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Substrates: very low specificity regarding size and chemical constitution of the accepted D-2-hydroxycarboxylates
Products: -
Products: -
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additional information
?
-
-
Substrates: the enzyme accepts D-2-hydroxyacids but not L-2-hydroxyacids and shows no NADP-dependent 2-ketopantoate reductase activity. No reactions are observed with 10 mM L-2-hydroxyisocaproate and 1 mM NAD+, 10 mM pyruvate and 0.3 mM NADH, 10 mM 2-oxooisocaproate and 0.3 mM NADPH, and 10 mM 2-oxopantoate and 0.3 mM NADH or NADPH
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme accepts D-2-hydroxyacids but not L-2-hydroxyacids and shows no NADP-dependent 2-ketopantoate reductase activity. No reactions are observed with 10 mM L-2-hydroxyisocaproate and 1 mM NAD+, 10 mM pyruvate and 0.3 mM NADH, 10 mM 2-oxooisocaproate and 0.3 mM NADPH, and 10 mM 2-oxopantoate and 0.3 mM NADH or NADPH
Products: -
Products: -
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additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant the proteins derived from the Escherichia coli cells harboring plasmids pET28a/ldh0076, pET28a/ldh1837, and pET28a/ldh2043 do not show any enzymatic activity toward pyruvate, D-lactate, or L-lactate, indicating that they are not LDHs that catalyze the interconversion of pyruvate and lactate. All three proteins exhibit NADH-oxidation activity toward oxaloacetate and 2-oxobutyrate, producing malate and 2-hydroxybutyrate, respectively. The protein encoded by LEUM_0076 shows clear NAD+-reduction activity toward L-malate, producing oxaloacetate, whereas the other two proteins encoded by LEUM_1837 and LEUM_2043 display NAD+-reduction activity toward D-malate, producing oxaloacetate
Products: -
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
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
Substrates: -
Products: -
Products: -
r
(R)-2-hydroxycarboxylate + NAD+
a 2-oxocarboxylate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
D-malate + NAD+
oxaloacetate + NADH + H+
Substrates: -
Products: -
Products: -
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
with NADP+ no reaction was observed in concentrations up to 4.5 mM
NAD+
enzyme binding structure analysis, overview
NADH
-
NADH can not be replaced by NADPH in the benzoylformate reduction by D-mandelate dehydrogenase D-ManDH1 or D-ManDH2
NADH
rhe enzyme requires NADH as a coenzyme for the hydrogenation reaction, NADPH does not support the reaction in concentrations up to 0.1 mM
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
no influence on the enzymatic activity can be detected with Mg2+ and Ca2+ and only very weak effects with Cd2+, Co2+ , and Mn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
10 mM, decrease of 13% in the enzymatic activity
additional information
the addition of citrate and EDTA (up to 10 mM) has no effect on the enzymatic activity. The addition of of iodoacetamide, KCN, 2-mercaptoethanol, dithiothreitol, and reduced glutathione in concentrations up to 20 mM has no effect
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.3
(R)-2-hydroxy-4-methylpentanoate
-
pH 7.0, temperature not specified in the publication
2.7
2-hydroxyhexanoate
-
pH 7.0, temperature not specified in the publication
1.6
2-Hydroxyoctanoate
-
pH 7.0, temperature not specified in the publication
3.3
2-hydroxypentanoate
-
pH 7.0, temperature not specified in the publication
0.12
2-oxooctanoate
-
pH 7.0, temperature not specified in the publication
0.6
3-(4-hydroxyphenyl)-2-oxopropanoate
-
pH 7.0, temperature not specified in the publication
2.9
3-hydroxypyruvate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
additional information
additional information
Michaelis-Menten kinetics, recombinant enzyme
-
3.4
2-oxo-3-phenylpropanoate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.36
2-oxobutyrate
-
in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
0.13
2-Oxohexanoate
-
pH 7.0, temperature not specified in the publication
2.3
2-oxoisocaproate
-
in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
71
2-oxoisocaproate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
46
2-oxoisovalerate
-
in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
0.12
2-oxopentanoate
-
pH 7.0, temperature not specified in the publication
0.15
3-methyl-2-oxobutanoate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.11
4-methyl-2-oxopentanoate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.4
4-methyl-2-oxopentanoate
-
pH 7.0, temperature not specified in the publication
0.05
NADH
-
with 2-oxobutyrate as cosubstrate, in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
0.086
NADH
-
with 2-oxoisocaproate as cosubstrate, in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
0.096
NADH
-
with pyruvate as cosubstrate, in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
0.26
phenylglyoxylate
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
0.0591
phenylpyruvate
recombinant His-tagged enzyme, pH and temperature not specified in the publication
0.2
phenylpyruvate
-
pH 7.0, temperature not specified in the publication
0.56
pyruvate
-
in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
43
(R)-2-hydroxy-4-methylpentanoate
-
pH 7.0, temperature not specified in the publication
26
2-hydroxyhexanoate
-
pH 7.0, temperature not specified in the publication
15
2-Hydroxyoctanoate
-
pH 7.0, temperature not specified in the publication
24
2-hydroxypentanoate
-
pH 7.0, temperature not specified in the publication
139
2-Oxohexanoate
-
pH 7.0, temperature not specified in the publication
1200
2-oxooctanoate
-
pH 7.0, temperature not specified in the publication
197
2-oxopentanoate
-
pH 7.0, temperature not specified in the publication
788
3-(4-hydroxyphenyl)-2-oxopropanoate
-
pH 7.0, temperature not specified in the publication
84
4-methyl-2-oxopentanoate
-
pH 7.0, temperature not specified in the publication
8.48
phenylpyruvate
recombinant His-tagged enzyme, pH and temperature not specified in the publication
968
phenylpyruvate
-
pH 7.0, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18
(R)-2-hydroxy-4-methylpentanoate
-
pH 7.0, temperature not specified in the publication
9.7
2-hydroxyhexanoate
-
pH 7.0, temperature not specified in the publication
25
2-Hydroxyoctanoate
-
pH 7.0, temperature not specified in the publication
7.2
2-hydroxypentanoate
-
pH 7.0, temperature not specified in the publication
1100
2-Oxohexanoate
-
pH 7.0, temperature not specified in the publication
139
2-oxooctanoate
-
pH 7.0, temperature not specified in the publication
1600
2-oxopentanoate
-
pH 7.0, temperature not specified in the publication
1300
3-(4-hydroxyphenyl)-2-oxopropanoate
-
pH 7.0, temperature not specified in the publication
210
4-methyl-2-oxopentanoate
-
pH 7.0, temperature not specified in the publication
4800
phenylpyruvate
-
pH 7.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.427
-
with 2-oxoisocaproate as substrate, in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
0.799
-
with 2-oxobutyrate as substrate, in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
1.462
-
with pyruvate as substrate, in 0.1 M glycine-NaOH buffer, pH 9.0, 4 M NaCl, at 52°C
170
-
after 77fold purification, in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
2.2
-
crude extract, in 100 mM Tris-HC1 buffer, pH 8.0, at 30°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
5.5 - 7
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 55
-
at 37°C, the activity reaches about 65% of peak activity at 55°C
65 - 75
-
above 60°C there is a pronounced activity decrease, while there is nearly no activity at 75°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
the enzyme belongs to the the NAD-dependent dehydrogenase family. Comparison with closely related members of the NAD-dependent dehydrogenase family reveals that whilst the D2-HDH core fold is structurally conserved, the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme. The protein, 2-hydroxyisocaproate dehydrogenase (HO-HxoDH), is virtually identical to the D2-HDH, with only three amino-acid differences between the two proteins, all at sites not known to be biologically relevant
evolution
-
the enzyme belongs to the the NAD-dependent dehydrogenase family. Comparison with closely related members of the NAD-dependent dehydrogenase family reveals that whilst the D2-HDH core fold is structurally conserved, the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme. The protein, 2-hydroxyisocaproate dehydrogenase (HO-HxoDH), is virtually identical to the D2-HDH, with only three amino-acid differences between the two proteins, all at sites not known to be biologically relevant
-
malfunction
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevents KIC reduction to 2-hydroxyisocaproate and slightly decreases the production of isovalerate
malfunction
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevented 4-methyl-2-oxopentanoate reduction to 2-hydroxyisocaproate and slightly decreased the production of isovalerate
malfunction
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevents KIC reduction to 2-hydroxyisocaproate and slightly decreases the production of isovalerate
-
malfunction
Lactococcus cremoris TIL46
-
the inactivation of panE does not affect the total percentage of leucine degraded but totally prevented 4-methyl-2-oxopentanoate reduction to 2-hydroxyisocaproate and slightly decreased the production of isovalerate
-
metabolism
-
its probable physiological role is to regenerate the NAD+ necessary to catabolize branched-chain amino acids, leading to the production of ATP and aroma compounds responsible for the reduction of the 2-keto acids derived from leucine, isoleucine, and valine
metabolism
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
Lactococcus cremoris TIL46
-
its probable physiological role is to regenerate the NAD+ necessary to catabolize branched-chain amino acids, leading to the production of ATP and aroma compounds responsible for the reduction of the 2-keto acids derived from leucine, isoleucine, and valine
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
metabolism
-
in Leuconostoc mesenteroides strain ATCC 8293, which lacks an L-ldh gene, L-lactate is produced through sequential enzymatic conversions from phosphoenolpyruvate to oxaloacetate, then L-malate, and finally L-lactate by phosphoenolpyruvate carboxylase (PEPC, gene ppcA, UniProt ID Q03VI7, LEUM_1694), L-MDH, and malolactic enzyme (MLE, UniProt ID Q03XG6, LEUM_1005), respectively
-
physiological function
the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme
physiological function
-
the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme
-
additional information
enzyme three-dimensional structure analysis, active site and cofactor binding site structures, overview
additional information
-
enzyme three-dimensional structure analysis, active site and cofactor binding site structures, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q03V58_LEUMM
Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y)
329
0
36215
TrEMBL
-
Q1GAA2_LACDA
Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14)
333
0
36849
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
37000
40000
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
additional information
homodimer
Lactiplantibacillus plantarum ATCC 8041
-
2 * 37183, calculated from amino acid sequence
-
additional information
enzyme three-dimensional structure analysis, overview
additional information
-
enzyme three-dimensional structure analysis, overview
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals are grown from a 1:1 mixture of a protein solution (10 mg/ml in 10 mM TrisHCl (pH 7.5)) and a reservoir solution (0.085 M HEPES-Na (pH 7.5), 0.17 M ammonium acetate and 22.5% PEG8000) using the hanging-drop vapor diffusion method at 25°C. The overall structure shows that the enzyme has a similar fold to 2-ketopantoate reductase, which catalyzes the conversion of 2-ketopantoate to D-pantoate using NADP+ as a coenzyme. They share conserved catalytic residues, indicating that D-mandelate dehydrogenase ManDH2 has the same reaction mechanism as 2-ketopantoate reductase. However, D-mandelate dehydrogenase ManDH2 exhibits significant structural variations in the coenzyme and substrate binding sites compared to 2-ketopantoate reductase. These structural observations can explain their different coenzyme and substrate specificities
hanging drop vapor diffusion method, using 2.0-3.5 M ammonium sulfate or 14-26% PEG 3350 as precipitant
-
hexagonal crystals of recombinant D-HicDH in the presence of NAD+ and 2-oxoisocaproate (4-methyl-2-oxopentanoate) are grown with ammonium sulfate as precipitating agent. The structure of the crystals is solved by molecular replacement and refined to a final R-factor of 19.6% for all measured X-ray reflections in the resolution range 1.9 A resolution
vapor diffusion using ammonium sulfate as precipitant. The crystals belong to hexagonal space group type P6(3)22 with a = b = 134.1 A, c = 124.1 A and diffract X-rays to 3.0 A resolution. Packing considerations show that there are either one or two D-HicDH monomers in the asymmetric unit
purified enzyme in apoform and complexed with coenzyme NAD+, hanging drop vapor diffusion method, mixing of 400 nl of 10 mg/ml protein in 40 mM HEPES, pH 7.4, 300 mM NaCl, and 0.02% v/v monothioglycerol, with 400 nl reservoir solution containing 25% PEG 3350, 200 mM MgCl2, 100 mM HEPES, pH 7.5, and equilibration against 0.1 ml of reservoir solution at 19°C, crystals are supplemented with 10 mM NAD+ for the enzyme complex crystals, X-ray diffraction structure determination at 3.45 A and 2.75 A resolution, respectively, molecular replacement and modeling using the monomer structure of D-2-hydroxyisocaproate dehydrogenase (D-HicDH) from Lactobacillus casei, PDB ID 1DXY
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.3 - 9.7
6 weeks, more than 80% of the activity is recovered
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
at temperatures above 50°C the stability of the enzyme decreases drastically
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, concentrated enzyme solution at pH 7.0 (10.6 mg/ml), 3 months, without significant loss of activity
-
4°C, diluted enzyme solution at pH 7.0 (0.004 mg/ml), 1 h, 40% loss of activity
-
4°C, pH 7.0, concentrated enzyme solution (10.6 mg/ml) is stable for at least 2-3 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose DE32 column chromatography, AMP-Sepharose column chromatography, and Mono Q column chromatography
-
recombinant His-tagged D2-HDH from Escherichia coli BL21(DE3) pLysS by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Sepharose column chromatography, DEAE-cellulose column chromatography, Q-Sepharose column chromatography, Sephacryl S-300 gel filtration, and Sephadex G25 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene Ldb1010, recombinant expression of His-tagged D2-HDH in Escherichia coli BL21(DE3) pLysS. The enzyme containing the non-native C-terminal hexahistidine tag and a 4-residue linker (Thr Ala Ser Gly linker) is enzymatically active
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), coexpression with genes ldh1837 and ldh2043
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
the enzyme can be utilized for preparation of enantiomerically pure (R)-2-hydroxy-4-methylpentanoate in 88% yield, using formate dehydrogenase recycling of the NADH coenzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, T.; Yang, W.; Pereira, A.C.; Craigen, W.J.; Shih, V.E.
Cloning and characterization of a putative human D-2-hydroxyacid dehydrogenase in chromosome 9q
Biochem. Biophys. Res. Commun.
268
298-301
2000
Homo sapiens
brenda
Bonete, M.J.; Ferrer, J.; Pire, C.; Penades, M.; Ruiz, J.L.
2-Hydroxyacid dehydrogenase from Haloferax mediteranii, a D-isomer-specific member of the 2-dehydrogenase family
Biochimie
82
1143-1150
2000
Haloferax mediterranei, Haloferax mediterranei R4, ATCC 33500
brenda
Wada, Y.; Iwai, S.; Tamura, Y.; Ando, T.; Shinoda, T.; Arai, K.; Taguchi, H.
A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases
Biosci. Biotechnol. Biochem.
72
1087-1094
2008
Enterococcus faecalis
brenda
Domenech, J.; Baker, P.; Sedelnikova, S.; Rodgers, H.; Rice, D.; Ferrer, J.
Crystallization and preliminary X-ray analysis of D-2-hydroxyacid dehydrogenase from Haloferax mediterranei
Acta Crystallogr. Sect. F
65
415-418
2009
Haloferax mediterranei, Haloferax mediterranei ATCC 335500
brenda
Chambellon, E.; Rijnen, L.; Lorquet, F.; Gitton, C.; Van Hylckama Vlieg, J.; Wouters, J.; Yvon, M.
The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis
J. Bacteriol.
191
873-881
2009
Lactococcus cremoris, Lactococcus cremoris TIL46, Lactococcus lactis, Lactococcus lactis IL1403
brenda
Taguchi, H.; Ohta, T.
D-lactate dehydrogenase is a member of the D-isomer-specific 2-hydroxyacid dehydrogenase family: Cloning, sequencing, and expression in Escherichia coli of the D-lactate dehydrogenase gene of Lactobacillus plantarum
J. Biol. Chem.
266
12588-12594
1991
Lactiplantibacillus plantarum, Lactiplantibacillus plantarum ATCC 8041
brenda
Niefind, K.; Hecht, H.J.; Schomburg, D.
Crystallization and preliminary characterization of crystals of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei
J. Mol. Biol.
240
400-402
1994
Lacticaseibacillus paracasei (P17584)
brenda
Dengler, U.; Niefind, K.; Kiess, M.; Schomburg, D.
Crystal structure of a ternary complex of D-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei, NAD+ and 2-oxoisocaproate at 1.9 A resolution
J. Mol. Biol.
267
640-660
1997
Lacticaseibacillus paracasei (P17584)
brenda
Tamura, Y.; Ohkubo, A.; Iwai, S.; Wada, Y.; Shinoda, T.; Arai, K.; Mineki, S.; Iida, M.; Taguchi, H.
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
Appl. Environ. Microbiol.
68
947-951
2002
Enterococcus faecalis
brenda
Miyanaga, A.; Fujisawa, S.; Furukawa, N.; Arai, K.; Nakajima, M.; Taguchi, H.
The crystal structure of D-mandelate dehydrogenase reveals its distinct substrate and coenzyme recognition mechanisms from those of 2-ketopantoate reductase
Biochem. Biophys. Res. Commun.
439
109-114
2013
Enterococcus faecium (E3USM3)
brenda
Hummel, W.; Schtte, H.; Kula, M.-R.
D-2-Hydroxyisocaproate dehydrogenase from Lactobacillus casei
Appl. Microbiol. Biotechnol.
21
7-15
1985
Lacticaseibacillus paracasei (P17584)
-
brenda
Kallwass, H.K.W.
Potential of R-2-hydroxyisocaproate dehydrogenase from Lactobacillus casei for stereospecific reductions
Enzyme Microb. Technol.
14
28-35
1992
Lacticaseibacillus casei
-
brenda
Bernard, N.; Johnsen, K.; Ferain, T.; Garmyn, D.; Hols, P.; Holbrook, J.J.; Delcour, J.
NAD(+)-dependent D-2-hydroxyisocaproate dehydrogenase of Lactobacillus delbrueckii subsp. bulgaricus. Gene cloning and enzyme characterization
Eur. J. Biochem.
224
439-446
1994
Lactobacillus delbrueckii (Q48534), Lactobacillus delbrueckii
brenda
Holton, S.; Anandhakrishnan, M.; Geerlof, A.; Wilmanns, M.
Structural characterization of a D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus
J. Struct. Biol.
181
179-184
2013
Lactobacillus delbrueckii subsp. bulgaricus (Q1GAA2), Lactobacillus delbrueckii subsp. bulgaricus ATCC 11842 (Q1GAA2)
brenda
Kim, K.H.; Jia, X.; Jia, B.; Jeon, C.O.
Identification and characterization of the L-malate dehydrogenases and L-lactate biosynthetic pathway in Leuconostoc mesenteroides ATCC 8293
J. Agric. Food Chem.
66
8086-8093
2018
Leuconostoc mesenteroides subsp. mesenteroides (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides 37Y (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides ATCC 8293 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides BCRC 11652 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides CCM 1803 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides DSM 20343 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides JCM 6124 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides NBRC 100496 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides NCDO 523 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides NCIMB 8023 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides NCTC 12954 (Q03V58), Leuconostoc mesenteroides subsp. mesenteroides NRRL B-1118 (Q03V58)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.345)
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