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Information on EC 1.1.1.37 - malate dehydrogenase and Organism(s) Drosophila melanogaster

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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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Drosophila melanogaster
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
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
-
-
-
-
L-malate dehydrogenase
-
-
-
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malate (NAD) dehydrogenase
-
-
-
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malate dehydrogenase (NAD)
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-
-
-
malic acid dehydrogenase
-
-
-
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malic dehydrogenase
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-
-
-
mbNAD-MDH
-
-
-
-
mNAD-MDH
-
-
-
-
NAD-dependent malate dehydrogenase
-
-
-
-
NAD-dependent malic dehydrogenase
-
-
-
-
NAD-L-malate dehydrogenase
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-
-
-
NAD-linked malate dehydrogenase
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-
-
-
NAD-malate dehydrogenase
-
-
-
-
NAD-malic dehydrogenase
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-
-
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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
-
-
-
-
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5
-
oxaloacetate reduction
9
-
malate oxidation, cytoplasmic isoenzymes
9.5
-
mitochondrial isoenzyme
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Oregon K
-
-
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?
Q9VU29_DROME
347
0
36737
TrEMBL
Mitochondrion (Reliability: 4)
Q8T8X0_DROME
349
0
36798
TrEMBL
Secretory Pathway (Reliability: 5)
Q8T412_DROME
347
0
36737
TrEMBL
Mitochondrion (Reliability: 3)
Q9VEB1_DROME
336
0
35318
TrEMBL
Mitochondrion (Reliability: 5)
B5RJP8_DROME
358
0
37866
TrEMBL
Secretory Pathway (Reliability: 1)
Q8MQS7_DROME
337
0
36073
TrEMBL
other Location (Reliability: 5)
Q9VKX2_DROME
337
0
36059
TrEMBL
other Location (Reliability: 5)
Q9VU28_DROME
349
0
36784
TrEMBL
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68000
-
both isoenzymes, gel filtration
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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