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Information on EC 1.1.1.37 - malate dehydrogenase and Organism(s) Plasmodium falciparum
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1.1.1.37 malate dehydrogenaseIUBMB 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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Word Map
- 1.1.1.37
- succinate
- isocitrate
- citrate
- isoenzymes
- oxaloacetate
- isozyme
- glucose-6-phosphate
-
tricarboxylic
- aminotransferase
- phosphoenolpyruvate
- carboxylase
- hexokinase
- dismutase
- esterase
- tca
- alpha-ketoglutarate
- creatine
- fumarase
- aldolase
-
carboxykinase
- transaminase
-
krebs
- phosphoglucomutase
- aconitase
- gpi
-
horn
-
citric
-
medullary
-
phosphofructokinase
- 6-phosphogluconate
-
nadp-dependent
-
trigeminal
-
1.1.1.27
-
allozyme
- meloidogyne
- glyoxysomal
- groes
-
nadp-malate
- alpha-glycerophosphate
- watermelon
-
phosphoglucose
- pqq
-
monomorphic
-
second-stage
-
isoenzymatic
-
root-knot
-
perineal
- diagnostics
- drug development
- biotechnology
- analysis
-
subnucleus
-
quinoproteins
- medicine
- agriculture
-
shsps
The taxonomic range for the selected organisms is: Plasmodium falciparum
The enzyme appears in selected viruses and cellular organisms
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-2-hydroxyacid dehydrogenase
-
-
-
-
L-malate dehydrogenase
malate (NAD) dehydrogenase
-
-
-
-
malate dehydrogenase (NAD)
-
-
-
-
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
-
-
-
-
VEG69
-
-
-
-
Vegetative protein 69
-
-
-
-
L-malate dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
Biosynthesis of secondary metabolites, Carbon fixation in photosynthetic organisms, Carbon fixation pathways in prokaryotes, Citrate cycle (TCA cycle), Cysteine and methionine metabolism, Glyoxylate and dicarboxylate metabolism, Methane metabolism, Microbial metabolism in diverse environments, Pyruvate metabolism
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
9001-64-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-malate + 3-acetylpyridine-adenine dinucleotide
oxaloacetate + reduced 3-acetylpyridine-adenine dinucleotide + H+
-
can also use 3-acetylpyridine-adenine as cofactor
-
-
r
(S)-malate + acetylpyridine adenine dinucleotide
oxaloacetate + reduced acetylpyridine adenine dinucleotide
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
highly specific for oxaloacetate and malate
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-malate + 3-acetylpyridine-adenine dinucleotide
oxaloacetate + reduced 3-acetylpyridine-adenine dinucleotide + H+
-
can also use 3-acetylpyridine-adenine as cofactor
-
-
r
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
highly specific for oxaloacetate and malate
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
-
enzymatically active preparation of recombinant wild type MDH, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tripathi, A.K.; Desai, P.V.; Pradhan, A.; Khan, S.I.; Avery, M.A.; Walker, L.A.; Tekwani, B.L.
An a-proteobacterial type malate dehydrogenase may complement LDH function in Plasmodium falciparum: Cloning and biochemical characterization of the enzyme
Eur. J. Biochem.
271
3488-3502
2004
Plasmodium falciparum (Q6VVP7), Plasmodium falciparum
EXTERNAL LINKS (specific for EC-Number 1.1.1.37)
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