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Information on EC 1.1.1.37 - malate dehydrogenase and Organism(s) Corynebacterium glutamicum and UniProt Accession Q8NN33
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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: Corynebacterium glutamicum
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
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-
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L-malate dehydrogenase
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-
-
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malate (NAD) dehydrogenase
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-
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malate dehydrogenase (NAD)
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-
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malic acid dehydrogenase
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-
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malic dehydrogenase
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-
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mbNAD-MDH
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-
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mNAD-MDH
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-
-
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NAD-dependent malate dehydrogenase
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-
-
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NAD-dependent malic dehydrogenase
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-
-
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NAD-L-malate dehydrogenase
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-
-
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NAD-linked malate dehydrogenase
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-
-
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NAD-malate dehydrogenase
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-
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NAD-malic dehydrogenase
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-
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NAD-specific malate dehydrogenase
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-
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VEG69
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-
-
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Vegetative protein 69
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
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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
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
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
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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
additional information
?
-
-
determination of intracellular NAD+/NADH ratios
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-
-
additional information
?
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determination of intracellular NAD+/NADH ratios
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-
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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
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
almost equally active both for NADH and NADPH on the bases of the turnover number values at pH 6.5, which is optimal for both coenzymes
NADH
almost equally active both for NADH and NADPH on the bases of the turnover number values at pH 6.5, which is optimal for both coenzymes
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(NH4)2SO4
reduction of oxaloacetate to malate and oxidation of malate to oxaloacetate
2-oxoglutarate
reduction of oxaloacetate to malate and oxidation of malate to oxaloacetate
NADH
-
MDH activity is strongly inhibited by excess of oxaloacetate and NADH over 1 mM
oxaloacetate
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MDH activity is strongly inhibited by excess of oxaloacetate and NADH over 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10.5
oxidation of L-malate to oxalacetete with NAD+ as coenzyme
6.5
reduction of oxaloacetate to L-malate with NADH as coenzyme, at oxaloacetate concentration of 0.05 mM. Reduction of oxalacetate to L-malate with NADPH as coenzyme
8
reduction of oxaloacetate to L-malate with NADH as coenzyme, at oxaloacetate concentration of 0.1 mM
9.5
reduction of oxaloacetate to L-malate with NADH as coenzyme, at oxaloacetate concentration of 1.0 mM
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
in glucose minimal medium, the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR. Ndh, Mdh and LdhA together cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
metabolism
the oxidation of NADH with the concomitant reduction of a quinone is a crucial step in the metabolism of respiring cells. Relevance of three different NADH oxidation systems in the actinobacterial model organism Corynebacterium glutamicum: non-proton-pumping NADH dehydrogenase (Ndh), and NADH-oxidizing enzymes, L-lactate dehydrogenase (LdhA) and malate dehydrogenase (Mdh)
physiological function
the enzyme is required for oxidation of NADH. The net reaction of the Mdh-Mqo couple equals that of an Ndh and it can serve as an alternative NADH dehydrogenase, as Mdh reduces oxaloacetate with NADH to L-malate, and the membrane-associated malate:quinone oxidoreductase (Mqo) subsequently re-oxidizes L-malate back to oxaloacetate and reduces menaquinone (MK)
evolution
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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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
additional information
characterization of defined mutants lacking the non-proton-pumping NADH dehydrogenase Ndh (DELTAndh) and/or one of the alternative NADH-oxidizing enzymes, L-lactate dehydrogenase LdhA (DELTAldhA) and malate dehydrogenase Mdh (DELTAmdh). Together with the menaquinone-dependent L-lactate dehydrogenase LldD and malate:quinone oxidoreductase Mqo, the LdhA-LldD and Mdh-Mqo couples can functionally replace Ndh activity. In glucose minimal medium the DELTAndh mutant, but not the DELTAldhA and DELTAmdh strains, show reduced growth and a lowered NAD+/NADH ratio, in line with Ndh being the major enzyme for NADH oxidation. Growth of the double mutants DELTAndh/DELTAmdh and DELTAndh/DELTAldhA, but not of strain DELTAmdh/DELTAldhA, in glucose medium is stronger impaired than that of the DELTAndh mutant, supporting an active role of the alternative Mdh-Mqo and LdhA-LldD systems in NADH oxidation and menaquinone reduction. In L-lactate minimal medium the DELTAndh mutant grows better than the wild-type, probably due to a higher activity of the menaquinone-dependent L-lactate dehydrogenase LldD. The DELTAndh/DELTAmdh mutant fails to grow in L-lactate medium and acetate medium. Growth with L-lactate can be restored by additional deletion of sugR, suggesting that ldhA repression by the transcriptional regulator SugR prevented growth on L-lactate medium. Attempts to construct a DELTAndh/DELTAmdh/DELTAldhA triple mutant are not successful, suggesting that Ndh, Mdh and LdhA cannot be replaced by other NADH-oxidizing enzymes in Corynebacterium glutamicum
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mdh, recombinant expression of MDH in differently engineered Corynebacterium glutamicum strains
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Genda, T.; Nakamatsu, T.; Ozaki, H.
Purification and characterization of malate dehydrogenase from Corynebacterium glutamicum
J. Biosci. Bioeng.
95
562-566
2003
Corynebacterium glutamicum (Q8NN33), Corynebacterium glutamicum
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
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Maeda, T.; Koch-Koerfges, A.; Bott, M.
Relevance of NADH dehydrogenase and alternative two-enzyme systems for growth of Corynebacterium glutamicum with glucose, lactate, and acetate
Front. Bioeng. Biotechnol.
8
621213
2020
Corynebacterium glutamicum, Corynebacterium glutamicum (Q8NN33), Corynebacterium glutamicum LMG 3730 (Q8NN33), Corynebacterium glutamicum BCRC 11384 (Q8NN33), Corynebacterium glutamicum ATCC 13032, Corynebacterium glutamicum ATCC 13032 (Q8NN33), Corynebacterium glutamicum JCM 1318 (Q8NN33), Corynebacterium glutamicum NCIMB 10025 (Q8NN33), Corynebacterium glutamicum DSM 20300 (Q8NN33)
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