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Information on EC 1.1.1.37 - malate dehydrogenase and Organism(s) Rattus norvegicus

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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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Rattus norvegicus
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(R)-2-hydroxyacid dehydrogenase
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-
-
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L-malate dehydrogenase
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-
-
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malate (NAD) dehydrogenase
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-
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malate dehydrogenase (NAD)
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-
-
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malic acid dehydrogenase
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-
-
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malic dehydrogenase
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-
-
-
mbNAD-MDH
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-
-
-
mNAD-MDH
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-
-
-
NAD-dependent malate dehydrogenase
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-
-
-
NAD-dependent malic dehydrogenase
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-
-
-
NAD-L-malate dehydrogenase
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-
-
-
NAD-linked malate dehydrogenase
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-
-
-
NAD-malate dehydrogenase
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-
-
-
NAD-malic dehydrogenase
-
-
-
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NAD-specific malate dehydrogenase
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-
-
-
VEG69
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-
-
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Vegetative protein 69
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
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-
-
-
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
-
-
-
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r
oxaloacetate + NADH + H+
(S)-malate + NAD+
show the reaction diagram
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-
-
-
?
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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
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decreases activity under normal and pathological conditions
Cu2+
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0.01-0.4 mM, activity from ischemic tissue decreases more significantly compared to the control
oxaloacetate
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-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 0.075
NADH
0.04 - 0.05
oxaloacetate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.2
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reduiction of oxaloacetate, enzyme from ischemic rats
7.2 - 7.8
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reduction of oxaloacetate, enzyme from normal rats
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
activity decreases 2.7times in myocardium of rats with experimental ischemia. Ischemic tissue damage is accompanied by changes in activity and kinetic and regulatory characteristics of cytoplasmic NAD-MDH from rat heart. It probably results from conformational changes in the enzyme molecule during generation and activation of reactive oxygen species of free radical processes
Manually annotated by BRENDA team
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?
MDHM_RAT
338
0
35684
Swiss-Prot
Mitochondrion (Reliability: 2)
MDHC_RAT
334
0
36483
Swiss-Prot
Secretory Pathway (Reliability: 4)
Q0QF43_RAT
301
0
31693
TrEMBL
other Location (Reliability: 4)
A0A8I6A721_RAT
339
0
37131
TrEMBL
other Location (Reliability: 4)
A0A8I6ABC9_RAT
327
0
34569
TrEMBL
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71600
-
gel filtration
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, completely inactivated
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4°C, no appreciable loss in activity for up to 3 months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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
Crow, K.E.; Braggins, T.J.; Batt, R.D.; Hardman, M.J.
Rat liver cytosolic malate dehydrigenase: Purification, kinetic properties, role in control of free cytosolic NADH concentration
J. Biol. Chem.
257
14217-14225
1982
Gallus sp., Rattus norvegicus, Sus scrofa, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Crow, K.E.; Braggins, T.J.; Hardman, M.J.
Human liver cytosolic malate dehydrogenase: Purification, kinetic properties, and role in ethanol metabolism
Arch. Biochem. Biophys.
225
621-629
1983
Homo sapiens, Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Wiseman, M.S.; McKay, D.; Crow, K.E.; Hardman, M.J.
Rat liver mitochondrial malate dehydrogenase: Purification, kinetic properties, and role in ethanol metabolism
Arch. Biochem. Biophys.
290
191-196
1991
Homo sapiens, Rattus norvegicus, Sus scrofa, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Safonova, O.A.; Popova, T.N.; Artyukhov, V.G.; Matasova, L.V.
Function of cytoplasmic NAD-dependent malate dehydrogenase from rat myocardium under conditions of ischemia
Bull. Exp. Biol. Med.
140
25-28
2005
Rattus norvegicus
Manually annotated by BRENDA team