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Information on EC 1.1.1.37 - malate dehydrogenase and Organism(s) Flavobacterium frigidimaris and UniProt Accession Q25QU7

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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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This record set is specific for:
Flavobacterium frigidimaris
UNIPROT: Q25QU7
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The taxonomic range for the selected organisms is: Flavobacterium frigidimaris
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
-
-
-
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malate (NAD) dehydrogenase
-
-
-
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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
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-
-
-
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
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
NAD+ binds first to the enzyme and then oxaloacetate is consequently released randomly via an ordered via an ordered bi-bi mechanism
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
show the reaction diagram
-
-
-
-
ir
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
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
malate dehydrogenase is an oligomeric enzyme that catalyzes the reversible oxidation of malate to oxaloacetate in the presence of NAD+, MDH is an essential metabolic enzyme in the citric acid cycle
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-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
the relative activity for NAD+ to that of NADP+ is about 43.9%. pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of the coenzyme
NADH
-
pro-R stereospecificity for hydrogen transfer at the C4 position of the nicotinamide moiety of the coenzyme
NADP+
-
the relative activity for NAD+ to that of NADP+ is about 43.9%. No activity with NADPH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
BaCl2
-
1 mM, 24.9% inhibition
CaCl2
-
1 mM, 29.1% inhibition
CoCl2
-
1 mM, 39% inhibition
CuCl2
-
1 mM, 89.8% inhibition
EDTA
-
1 mM, 52.2% inhibition
HgCl2
-
1 mM, complete inhibition
hydroxylamine
-
1 mM, 57.1% inhibition
iodoacetate
-
1 mM, 93.6% inhibition
MgCl2
-
1 mM,34.9% inhibition
MnCl2
-
1 mM, 28.6% inhibition
NEM
-
1 mM, complete inhibition
NiCl2
-
1 mM, 36.8% inhibition
Semicarbazide
-
1 mM, 61.3% inhibition
ZnCl2
-
1 mM, 72.6% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.269 - 0.74
(S)-malate
0.0279 - 0.0382
NAD+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
41.3 - 138
(S)-malate
1.73 - 139
NAD+
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10.5
-
oxidation of malate
8
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reduction of oxaloacetate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 50
-
20°C: about 55% of maximal activity, 50°C: about 50% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MDH_FLAFR
311
0
32610
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
123000
-
gel filtration
32000
-
4 * 32000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 32000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
tetrameric enzyme, hanging drop vapour diffusion method, 15°C, 17 mg/ml protein in 10 mM potassium phosphate buffer, pH 7.0, equilibration of the 0.002 ml protein drop against 500 ml reservoir solution consisting of 1.4 M ammonium sulfate, 5% v/v MPD, 2 mM NAD+, 50 mM sodium citrate buffer, pH 5.5, 2-3 days, X-ray diffraction structure determination and analysis at 1.8 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10.5
-
stable
668012
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
half-life: 26 min
40
-
half-life: 3 min
45
-
half-life: 0.6 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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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
Manually annotated by BRENDA team
Fujii, T.; Oikawa, T.; Muraoka, I.; Soda, K.; Hata, Y.
Crystallization and preliminary X-ray diffraction studies of tetrameric malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium frigidimaris KUC-1
Acta Crystallogr. Sect. F
63
983-986
2007
Flavobacterium frigidimaris (Q25QU7), Flavobacterium frigidimaris, Flavobacterium frigidimaris KUC-1 (Q25QU7), Flavobacterium frigidimaris KUC-1
Manually annotated by BRENDA team