Information on EC 1.1.1.299 - malate dehydrogenase [NAD(P)+]

for references in articles please use BRENDA:EC1.1.1.299
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The expected taxonomic range for this enzyme is: Bacteria, Archaea

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EC NUMBER
COMMENTARY hide
1.1.1.299
-
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RECOMMENDED NAME
GeneOntology No.
malate dehydrogenase [NAD(P)+]
-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-malate + NAD(P)+ = oxaloacetate + NAD(P)H + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
citric acid cycle
-
-
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SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NAD(P)+ oxidoreductase
This enzyme, which was characterized from the methanogenic archaeon Methanobacterium thermoautotrophicum, catalyses only the reduction of oxaloacetate, and can use NAD+ and NADP+ with similar specific activity [1]. Different from EC 1.1.1.37 (malate dehydrogenase (NAD+)), EC 1.1.1.82 (malate dehydrogenase (NADP+)) and EC 1.1.5.4 (malate dehydrogenase (quinone)).
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CAS REGISTRY NUMBER
COMMENTARY hide
9001-64-3
cf. EC 1.1.1.37
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KUC-1
-
-
Manually annotated by BRENDA team
strain KUC-1
-
-
Manually annotated by BRENDA team
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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 + NADP+
oxaloacetate + NADPH + H+
show the reaction diagram
oxaloacetate + NADH
L-malate + NAD+
show the reaction diagram
-
-
-
-
?
oxaloacetate + NADH + H+
L-malate + NAD+
show the reaction diagram
-
-
-
-
?
oxaloacetate + NADPH
L-malate + NADP+
show the reaction diagram
-
-
-
-
?
additional information
?
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
additional information
-
no cofactor: NADPH
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CuCl2
-
1 mM, 10% residual activity
HgCl2
-
1 mM, no residual activity
iodoacetate
-
1 mM, 16.4% residual activity
N-ethylmaleimide
-
1 mM, no residual activity
NADH
-
inhibitory above 0.2 mM
NADPH
-
inhibitory above 0.2 mM
ZnCl2
-
1 mM, 27% residual activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.269 - 0.74
L-malate
0.028 - 0.5
NAD+
0.09
oxaloacetate
-
pH 7.6
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
41.3 - 138
L-malate
41 - 139
NAD+
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
289
L-malate
-
30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1
-
pH 7.6, oxidation of malate, cosubstrate NAD+; pH 7.6, oxidation of malate, cosubstrate NADP+
52
-
pH 7.6, reduction of oxaloacetate, cosubstrate NADP+
60
-
pH 7.6, reduction of oxaloacetate, cosubstrate NAD+
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
reduction of oxaloacetate
10.5
-
oxidation of malate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10
-
reduction of oxaloacetate
6.5 - 12
-
oxidation of malate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
highest initial velocity
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
4 * 32000, SDS-PAGE
36000
-
x * 36000, SDS-PAGE, x * 36700, calculated
36700
-
x * 36000, SDS-PAGE, x * 36700, calculated
123000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 36000, SDS-PAGE, x * 36700, calculated
tetramer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 10.5
-
-
668012
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
half-life 26 min
40
-
half-life 3 min
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.299)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)