Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.1.37 - malate dehydrogenase and Organism(s) Streptomyces coelicolor and UniProt Accession Q9K3J3

for references in articles please use BRENDA:EC1.1.1.37
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Streptomyces coelicolor
UNIPROT: Q9K3J3
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Streptomyces coelicolor
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
(S)-malate dehydrogenase
-
NAD+-dependent MDH
-
(R)-2-hydroxyacid dehydrogenase
-
-
-
-
L-malate dehydrogenase
-
-
-
-
L-malate:NAD oxidoreductase
-
-
malate (NAD) dehydrogenase
-
-
-
-
malate dehydrogenase (NAD)
-
-
-
-
malic acid dehydrogenase
-
-
-
-
malic dehydrogenase
-
-
-
-
mbNAD-MDH
-
-
-
-
mNAD-MDH
-
-
-
-
NAD+-dependent malate dehydrogenase
-
-
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
-
-
-
-
additional information
MDH belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases
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
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-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
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
show the reaction diagram
-
-
-
-
r
oxaloacetate + NADH + H+
(S)-malate + NAD+
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
dependent on and specific for
NADH
dependent on and specific for
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
enzyme activity is not or poorly affected by 2 mM of Ca2+, Mn2+, Cu2+, Mg2+, Na+, Li+, K+, Rb+, and Ag+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-malate
substrate inhibition, 60% inhibition at 30 mM
Co2+
36% inhibition at 2 mM
Fe2+
complete inhibition at 2 mM
oxaloacetate
substrate inhibition, 50% inhibition at 6 mM
Zn2+
73% inhibition at 2 mM
L-malate
-
MDH activity is strongly inhibited by excess of L-malate
oxaloacetate
-
MDH activity is strongly inhibited by excess of oxaloacetate
additional information
MDH is not affected by DTT or EDTA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
MDH is not affected by DTT or EDTA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.494
(S)-malate
pH 8.5, 30°C
0.15
NAD+
pH 8.5, 30°C
0.83
NADH
pH 8.5, 30°C
0.189
oxaloacetate
pH 8.5, 30°C
0.49
(S)-malate
-
pH and temperature not specified in the publication
0.15
NAD+
-
pH and temperature not specified in the publication
0.083
NADH
-
pH and temperature not specified in the publication
0.0189
oxaloacetate
-
pH and temperature not specified in the publication
additional information
additional information
-
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.71
(S)-malate
pH 8.5, 30°C
3.66
NAD+
pH 8.5, 30°C
542
NADH
pH 8.5, 30°C
1870
oxaloacetate
pH 8.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.53
(S)-malate
pH 8.5, 30°C
24.4
NAD+
pH 8.5, 30°C
6560
NADH
pH 8.5, 30°C
10000
oxaloacetate
pH 8.5, 30°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12.8
(S)-malate
pH 8.5, 30°C
5.8
oxaloacetate
pH 8.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8
50°C, phosphate buffer, recombinant enzyme, reduction and oxidation
8.5
30°C, Tris-HCl buffer, recombinant enzyme, reduction and oxidation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.7 - 10
profiles in different buffers, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
reduction and oxidation
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 60
profile, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mdh
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
mitochondrial and cytosolic MDH isozymes are required for maintaining the balance of NAD+ and NADH in mitochondria and cytosol
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
physiological function
-
regulation of MDH activity, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36675
73350
dimeric enzyme, MALDI-TOF mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 36675, MALDI-TOF mass spectrometry
tetramer
4 * 36675, MALDI-TOF mass spectrometry
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
20 min, purified recombinant enzyme, 82% activity remaining
50
purified recombinant enzyme, 70% activity remaining after 20 min, 71% after 30 min, 60% after 90 min, and 50% after 120 min
55
20 min, purified recombinant enzyme, 10% activity remaining
60
20 min, purified recombinant enzyme, complete inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged MDH from Escherichia coli strain Rosetta(DE3) by cobalt affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mdh, sequence comparisons and phylogenetic analysis, overview, overexpression of His6-tagged MDH in Escherichia coli strain Rosetta(DE3), subcloning in Escherichia coli strain DH5alpha
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcriptional regulation of mdh gene, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ge, Y.D.; Cao, Z.Y.; Wang, Z.D.; Chen, L.L.; Zhu, Y.M.; Zhu, G.P.
Identification and biochemical characterization of a thermostable malate dehydrogenase from the mesophile Streptomyces coelicolor A3(2)
Biosci. Biotechnol. Biochem.
74
2194-2201
2010
Streptomyces coelicolor (Q9K3J3), Streptomyces coelicolor A3(2) (Q9K3J3), Streptomyces coelicolor A3(2)
Manually annotated by BRENDA team
Takahashi-Iniguez, T.; Aburto-Rodriguez, N.; Vilchis-Gonzalez, A.; Flores, M.
Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase
J. Zhejiang Univ. Sci. B
17
247-261
2016
Aeropyrum pernix, Archaeoglobus fulgidus, Bacillus subtilis, uncultured bacterium, Corynebacterium glutamicum, Escherichia coli, Glaesserella parasuis, Haloarcula marismortui, Helicobacter pylori, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Nitrosomonas europaea, Pseudomonas stutzeri, Kitasatospora aureofaciens, Streptomyces coelicolor, uncultured bacterium MPOB, Bacillus subtilis B1
-
Manually annotated by BRENDA team