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Information on EC 1.1.1.37 - malate dehydrogenase and Organism(s) Sulfolobus acidocaldarius and UniProt Accession P11386
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1.1.1.37 malate dehydrogenaseIUBMB Comments
There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme forms oxaloacetate and unlike EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. EC 1.1.1.82, malate dehydrogenase (NADP+); EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and EC 1.1.5.4, malate dehydrogenase (quinone).
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Word Map
- 1.1.1.37
- succinate
- isocitrate
- citrate
- isoenzymes
- oxaloacetate
- isozyme
- glucose-6-phosphate
-
tricarboxylic
- aminotransferase
- phosphoenolpyruvate
- carboxylase
- hexokinase
- dismutase
- esterase
- tca
- alpha-ketoglutarate
- creatine
- fumarase
- aldolase
-
carboxykinase
- transaminase
-
krebs
- phosphoglucomutase
- aconitase
- gpi
-
horn
-
citric
-
medullary
-
phosphofructokinase
- 6-phosphogluconate
-
nadp-dependent
-
trigeminal
-
1.1.1.27
-
allozyme
- meloidogyne
- glyoxysomal
- groes
-
nadp-malate
- alpha-glycerophosphate
- watermelon
-
phosphoglucose
- pqq
-
monomorphic
-
second-stage
-
isoenzymatic
-
root-knot
-
perineal
- diagnostics
- drug development
- biotechnology
- analysis
-
subnucleus
-
quinoproteins
- medicine
- agriculture
-
shsps
The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
malate dehydrogenase, mdh, mitochondrial malate dehydrogenase, malic dehydrogenase, cytosolic malate dehydrogenase, maldh, nad-dependent malate dehydrogenase, mitochondrial mdh, s-mdh, l-malate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-2-hydroxyacid dehydrogenase
-
-
-
-
L-malate dehydrogenase
-
-
-
-
malate (NAD) dehydrogenase
-
-
-
-
malate dehydrogenase (NAD)
-
-
-
-
malic acid dehydrogenase
-
-
-
-
malic dehydrogenase
-
-
-
-
mbNAD-MDH
-
-
-
-
mNAD-MDH
-
-
-
-
NAD-dependent malate dehydrogenase
-
-
-
-
NAD-dependent malic dehydrogenase
-
-
-
-
NAD-L-malate dehydrogenase
-
-
-
-
NAD-linked malate dehydrogenase
-
-
-
-
NAD-malate dehydrogenase
-
-
-
-
NAD-malic dehydrogenase
-
-
-
-
NAD-specific malate dehydrogenase
-
-
-
-
VEG69
-
-
-
-
Vegetative protein 69
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
Biosynthesis of secondary metabolites, Carbon fixation in photosynthetic organisms, Carbon fixation pathways in prokaryotes, Citrate cycle (TCA cycle), Cysteine and methionine metabolism, Glyoxylate and dicarboxylate metabolism, Methane metabolism, Microbial metabolism in diverse environments, Pyruvate metabolism
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NAD+ oxidoreductase
There are several forms of malate dehydrogenases that differ by their use of substrate and cofactors. This NAD+-dependent enzyme forms oxaloacetate and unlike EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating), is unable to convert it to pyruvate. Also oxidizes some other 2-hydroxydicarboxylic acids. cf. EC 1.1.1.82, malate dehydrogenase (NADP+); EC 1.1.1.299, malate dehydrogenase [NAD(P)+]; and EC 1.1.5.4, malate dehydrogenase (quinone).
CAS REGISTRY NUMBER
COMMENTARY
9001-64-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
low activity in this direction
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
the binding domain for NAD(H) is localized at the N-terminal part of the polypeptide chain
NADH
the binding domain for NAD(H) is localized at the N-terminal part of the polypeptide chain
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
product inhibition, 29% inhibition at 5 mM, 42% inhibition at 10 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
277
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
128500
134000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
activity of purified enzyme decreases continually from 4°C to 80°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, pH 7.0-9.0, concentration of 0.0018 mg/ml, quite stable. Below pH 7.0, inactivation occurs
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grossebueter, W.; Hartl, T.; Goerisch, H.; Stezowski, J.J.
Purification and properties of malate dehydrogenase from the thermophilic archaebacterium Thermoplasma acidophilum
Biol. Chem. Hoppe-Seyler
367
457-463
1986
Bacillus subtilis, Bacillus sp. (in: Bacteria), Halobacterium salinarum, Methanospirillum hungatei, Sulfolobus acidocaldarius, Thermoplasma acidophilum
Hartl, T.; Grossebueter, W.; Goerisch, H.; Stezowski, J.J.
Crystalline NAD/NADP-dependent malate dehydrogenase; the enzyme from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
Biol. Chem. Hoppe-Seyler
368
259-267
1987
Escherichia coli, Thermus thermophilus, Methanothermobacter thermautotrophicus, Methanospirillum hungatei, Sulfolobus acidocaldarius, Sus scrofa, Laceyella sacchari, Thermoplasma acidophilum, Thermus aquaticus
Tayeh, M.A.; Madigan, M.T.
Malate dehydrogenase in phototrophic purple bacteria: Purification, molecular weight, and quaternary structure
J. Bacteriol.
169
4196-4202
1987
Geobacillus stearothermophilus, [Bacillus] caldolyticus, Priestia megaterium, Bacillus subtilis, Bacillus sp. (in: Bacteria), Bos taurus, Brevibacterium sp., Corynebacterium sp., Escherichia coli, Halobacterium salinarum, Methanospirillum hungatei, no activity in Chromatium sp., Rhodobacter capsulatus, Rhodocyclus purpureus, Rhodomicrobium vannielii, Rhodopseudomonas palustris, Rhodospirillum rubrum, Sulfolobus acidocaldarius, Sus scrofa, Laceyella sacchari, Thermoplasma acidophilum, Rhodobacter capsulatus B100, Rhodocyclus purpureus 6770, Rhodospirillum rubrum 1.1.1, Rhodobacter capsulatus 37b4, Rhodomicrobium vannielii EY33
Tayeh, M.A.; Madigan, M.T.
Malate dehydrogenases in phototrophic purple bacteria. Thermal stability, amino acid composition and immunological properties
Biochem. J.
252
595-600
1988
Geobacillus stearothermophilus, Priestia megaterium, Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli, Methanospirillum hungatei, Rhodobacter capsulatus, Rhodocyclus purpureus, Rhodomicrobium vannielii, Rhodospirillum rubrum, Sulfolobus acidocaldarius, Sus scrofa, Thermoplasma acidophilum, Rhodobacter capsulatus B100, Rhodocyclus purpureus 6770, Rhodospirillum rubrum 1.1.1, Rhodomicrobium vannielii EY33
Musrati, R.A.; Kollarova, M.; Mernik, N.; Mikulasova, D.
Malate dehydrogenase: Distribution, function and properties
Gen. Physiol. Biophys.
17
193-210
1998
Saccharomyces cerevisiae, Citrullus lanatus, Escherichia coli, Eucalyptus globulus, Euglena gracilis, Thermus thermophilus, Haloarcula marismortui, Methanothermus fervidus, Mus musculus, Nitzschia alba, Rattus norvegicus, Kitasatospora aureofaciens, Sulfolobus acidocaldarius, Sus scrofa, Zea mays
Grisch, H.; Hartl, T.; Grossebter, W.; Stezowski, J.J.
Archaebacterial malate dehydrogenases. The enzymes from the thermoacidophilic organisms Sulfolobus acidocaldarius and Thermoplasma acidophilum show A-side stereospecificity for NAD+
Biochem. J.
226
885-888
1985
Sulfolobus acidocaldarius, Thermoplasma acidophilum
Stezowski, J.J.; Englmaier, R.; Galdiga, C.; Hartl, T.; Rommel, I.; Dauter, Z.; Grisch, H.; Grossebter, W.; Wilson, K.; Musil, D.
Preliminary X-ray crystallographic study of malate dehydrogenases from the thermoacidophilic Archaebacteria Thermoplasma acidophilum and Sulfolobus acidocaldarius
J. Mol. Biol.
208
507-508
1989
Sulfolobus acidocaldarius, Thermoplasma acidophilum
Goerisch, H.; Jany, K.D.
Archaebacterial malate dehydrogenase: the amino-terminal sequence of the enzyme from Sulfolobus acidocaldarius is homologous to the eubacterial and eukaryotic malate dehydrogenases
FEBS Lett.
247
259-262
1989
Sulfolobus acidocaldarius (P11386), Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DSM 639 (P11386)
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