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Information on EC 1.1.1.37 - malate dehydrogenase and Organism(s) Bos taurus

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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
                1.1.1.37 malate dehydrogenase
IUBMB 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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The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Synonyms
malate dehydrogenase, mdh, mitochondrial malate dehydrogenase, malic dehydrogenase, cytosolic malate dehydrogenase, nad-dependent malate dehydrogenase, maldh, mitochondrial mdh, s-mdh, l-malate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(R)-2-hydroxyacid dehydrogenase
-
-
-
-
L-malate dehydrogenase
-
-
-
-
malate (NAD) dehydrogenase
-
-
-
-
malate dehydrogenase (NAD)
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-
-
-
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 hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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 hide
9001-64-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
oxaloacetate + NADH
L-malate + NAD+
show the reaction diagram
-
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-fructose 1,6-diphosphate
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heart s-MDH, inhibits the binding of NADH
sulfite
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.6
-
oxaloacetate reduction, s-MDH
7.8
-
oxaloacetate reduction, m-MDH
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SERA_BOVIN
533
0
56452
Swiss-Prot
other Location (Reliability: 2)
MDHC_BOVIN
334
0
36438
Swiss-Prot
Secretory Pathway (Reliability: 5)
MDHM_BOVIN
338
0
35668
Swiss-Prot
Mitochondrion (Reliability: 2)
Q0QF29_BOVIN
284
0
29951
TrEMBL
Mitochondrion (Reliability: 5)
A0A452DIW4_BOVIN
329
0
35856
TrEMBL
Secretory Pathway (Reliability: 5)
Q58DR9_BOVIN
278
0
30024
TrEMBL
Mitochondrion (Reliability: 2)
A0A3Q1LTB0_BOVIN
312
0
33005
TrEMBL
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
s-MDH
62000
-
m-MDH
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
s-MDH
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McReynolds, M.S.; Barrie Kitto, G.
Purification and properties of Drosophila malate dehydrogenase
Biochim. Biophys. Acta
198
165-175
1970
Bos taurus, Drosophila melanogaster, Drosophila virilis, Equus sp., Gallus sp., Locusta migratoria, Sus scrofa, Thunnus albacares, Drosophila melanogaster Oregon K, Drosophila virilis Texmelucan
Manually annotated by BRENDA team
Teague, W.M.; Henney, H.R.
Purification and properties of cytoplasmic and mitochondria malate dehydrogenase of Physarum polycephalum
J. Bacteriol.
116
673-684
1973
Ascaris suum, Bos taurus, Saccharomyces cerevisiae, Auxenochlorella pyrenoidosa, Citrus sp., Drosophila virilis, Fundulus heteroclitus, Gallus sp., Tritia obsoleta, Neurospora crassa, Opuntia ficus-indica, Phycomyces blakesleeanus, Physarum polycephalum, Salmo sp., Spinacia oleracea, Strongylocentrotus purpuratus, Thunnus albacares, Zea mays
Manually annotated by BRENDA team
Banaszak, L.J.; Bradshaw, R.A.
Malate dehydrogenases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
11
369-396
1975
Geobacillus stearothermophilus, Bacillus subtilis, Bos taurus, Drosophila virilis, Escherichia coli, Equus sp., Gallus sp., Ovis aries, Neurospora crassa, Phycomyces blakesleeanus, Rattus norvegicus, Salmo sp., Sus scrofa, Thunnus albacares
-
Manually annotated by BRENDA team
You, K.S.; Kaplan, N.O.
Purification and properties of malate dehydrogenase from Pseudomonas testosteroni
J. Bacteriol.
123
704-716
1975
Geobacillus stearothermophilus, Bacillus subtilis, Bos taurus, Delftia acidovorans, Comamonas testosteroni, Escherichia coli, Equus sp., Solanum tuberosum, Sus scrofa, Triticum aestivum
Manually annotated by BRENDA team
Teague, W.M.; Henney, H.R.
Physical properties and chemical compositions of cytoplasmic and mitochondrial malate dehydrogenase from Physarum polycephalum
Biochim. Biophys. Acta
434
118-125
1976
Bos taurus, Gallus sp., Penaeus aztecus, Physarum polycephalum, Salmo sp., Sus scrofa
Manually annotated by BRENDA team
Mevarech, M.; Eisenberg, H.; Neumann, E.
Malate dehydrogenase isolated from extremely halophilic bacteria of the dead sea. 1. Purification and molecular characterization
Biochemistry
16
3781-3785
1977
Bacillus subtilis, Bos taurus, Comamonas testosteroni, Escherichia coli, Halobacterium salinarum, Sus scrofa, Thermus aquaticus
Manually annotated by BRENDA team
Tyagi, A.K.; Siddiqui, F.A.; Venkitasubramanian, T.A.
Studies on the purification and characterization of malate dehydrogenase from Mycobacterium phlei
Biochim. Biophys. Acta
485
255-267
1977
Bacillus subtilis, Bos taurus, Escherichia coli, Homo sapiens, Mycobacterium tuberculosis, Mycobacterium kansasii, Mycolicibacterium phlei, Mycobacterium scrofulaceum, Neurospora crassa, no activity in Mycobacterium fortuitum, no activity in Mycobacterium smegmatis, no activity in Mycobacterium smegmatis 607
Manually annotated by BRENDA team
Storer, A.C.; Sprott, G.D.; Martin, W.G.
Kinetic and physical properties of the L-malate-NAD+ oxidoreductase from Methanospirillum hungatii and comparison with the enzyme from other sources
Biochem. J.
193
235-244
1981
Bacillus subtilis, Bos taurus, Saccharomyces cerevisiae, Comamonas testosteroni, Escherichia coli, Equus sp., Thermus thermophilus, Gallus sp., Halobacterium salinarum, Methanospirillum hungatei, Mycobacterium sp., Mycolicibacterium phlei, Neurospora crassa, Rattus norvegicus, Salmo sp., Sus scrofa, Thermus aquaticus, Thunnus albacares, Methanospirillum hungatei GPI
Manually annotated by BRENDA team
Emyanitoff, R.G.; Kelly, P.J.
Kinetic characterization of Mitochondrial malate dehydrogenase from Dictyostelium discoideum
J. Gen. Microbiol.
128
1767-1771
1982
Bos taurus, Saccharomyces cerevisiae, Dictyostelium discoideum, Gallus sp., Physarum polycephalum, Schizosaccharomyces pombe, Sus scrofa, Dictyostelium discoideum NC-4 / ATCC 24697
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team