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Information on EC 1.1.1.299 - malate dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.299
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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
1.1.1.299 malate dehydrogenase [NAD(P)+]
IUBMB Comments
This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity . Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 (malate dehydrogenase (quinone)).
The expected taxonomic range for this enzyme is: Archaea, Bacteria
- 1.1.1.299
- maldhs
- dehydrogenases
- l-lactate
-
nad-dependent
- l-malate
-
hyperthermophilic
-
archaeon
showSynonyms
mdh ii, ldh-like maldh, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
-
-
-
-
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
ordered bi-bi mechanism
-
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
ordered bi-bi mechanism
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NAD(P)+ oxidoreductase
This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity [1].
Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 (malate dehydrogenase (quinone)).
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CAS REGISTRY NUMBER
COMMENTARY
9001-64-3
cf. EC 1.1.1.37
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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
oxaloacetate + NADH
L-malate + NAD+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH
L-malate + NADP+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
?
pyruvate + NADH + H+
?
-
Substrates: weak catalytic efficiency with pyruvate
Products: -
Products: -
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
Substrates: the enzyme strongly prefers oxaloacetate by three orders of magnitude compared to pyruvate
Products: -
Products: -
?
oxaloacetate + NADH + H+
L-malate + NAD+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADH + H+
L-malate + NAD+
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme shows pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of the coenzyme. No substrates are: D-malate, malonate, L-glutamate, L-aspartate, D,L-2-hydroxybutanoate, D,L-3-hydroxybutanoate, citrate, maleate, succinate, L-tartrate, L-threonine, L-serine, L-hydroxymalonate, D-glutamate, 2-oxocaproate, 2-oxoisovalerate, glyoxylate, 2-oxoglutarate, 2-oxobutanoate
Products: -
Products: -
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additional information
?
-
-
Substrates: no substrate: pyruvate
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
oxaloacetate + NADH + H+
(S)-malate + NAD+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52
-
pH 7.6, reduction of oxaloacetate, cosubstrate NADP+
60
-
pH 7.6, reduction of oxaloacetate, cosubstrate NAD+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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.
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). MDH_METTM
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)
325
0
35860
Swiss-Prot
-
MDH_METTH
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
325
0
35933
Swiss-Prot
-
MDH_METST
Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)
317
0
34857
Swiss-Prot
-
MDH_METMP
Methanococcus maripaludis (strain DSM 14266 / JCM 13030 / NBRC 101832 / S2 / LL)
314
0
34468
Swiss-Prot
-
MDH_METKA
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
317
0
34609
Swiss-Prot
other Location (Reliability: 2)
MDH_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
308
0
33490
Swiss-Prot
-
MDH_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
313
0
34609
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
124000
-
size exclusion chromatography-multi angle laser light scattering
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme, sitting drop vapor diffusion method, using 10% (w/v) PEG 6000 and 100 mM EPES at pH 7.0
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oikawa, T.; Yamamoto, N.; Shimoke, K.; Uesato, S.; Ikeuchi, T.; Fujioka, T.
Purification, characterization, and overexpression of psychrophilic and thermolabile malate dehydrogenase of a novel antarctic psychrotolerant, Flavobacterium frigidimaris KUC-1
Biosci. Biotechnol. Biochem.
69
2146-2154
2005
Flavobacterium frigidimaris, Flavobacterium frigidimaris KUC-1
brenda
Thompson, H.; Tersteegen, A.; Thauer, R.; Hedderich, R.
Two malate dehydrogenases in Methanobacterium thermoautotrophicum
Arch. Microbiol.
170
38-42
1998
Methanothermobacter thermautotrophicus
brenda
Roche, J.; Girard, E.; Mas, C.; Madern, D.
The archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization
J. Struct. Biol.
208
7-17
2019
Ignicoccus islandicus
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.299)
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Release 2026.1 (March 2026)
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