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IUBMB CommentsThere 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).
Synonyms
malate dehydrogenase, mdh, mitochondrial malate dehydrogenase, malic dehydrogenase, cytosolic malate dehydrogenase, nad-dependent malate dehydrogenase, maldh, mitochondrial mdh, s-mdh, l-malate dehydrogenase,
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(R)-2-hydroxyacid dehydrogenase
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cytosolic malate dehydrogenase
cytosolic malate dehydrogenase 1
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cytosolic NAD-dependent malate dehydrogenase
halophilic malate dehydrogenase
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L-malate-NAD oxidoreductase
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L-malate-NAD-oxidoreductase
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L-malate: NAD oxidoreductase
L-malate: NAD+ oxidoreductase
L-malate:NAD oxidoreductase
L-malate:NAD-oxidoreductase
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LDH-like malate dehydrogenase
malate (NAD) dehydrogenase
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malate dehydrogenase (NAD)
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malate dehydrogenase 1
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malate: NAD oxidoreductase
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malic acid dehydrogenase
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malic dehydrogenase
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mitochondrial malate dehydrogenase
NAD+ malate dehydrogenase
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NAD+-dependent malate dehydrogenase
NAD-dependent cytosolic malate dehydrogenase
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NAD-dependent malate dehydrogenase
NAD-dependent malic dehydrogenase
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NAD-L-malate dehydrogenase
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NAD-linked malate dehydrogenase
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NAD-malic dehydrogenase
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NAD-specific malate dehydrogenase
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NADP+-dependent malate dehydrogenase
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peroxisomal malate dehydrogenase
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peroxisomal NAD+-malate dehydrogenase 1
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peroxisomal NAD+-malate dehydrogenase 2
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plastid-localized NAD-dependent MDH
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plastidial NAD+-dependent malate dehydrogenase
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plastidial NAD-dependent malate dehydrogenase
plastidial NAD-dependent malate dehydrogenase 1
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regulatory subunit of nucleic acid-conducting channel
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Vegetative protein 69
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(S)-malate dehydrogenase

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(S)-malate dehydrogenase
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cMDH

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cMDH
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cytosolic isoenzyme
cytosolic malate dehydrogenase

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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic malate dehydrogenase
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cytosolic NAD-dependent malate dehydrogenase

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cytosolic NAD-dependent malate dehydrogenase
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L-malate dehydrogenase

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L-malate dehydrogenase
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L-malate dehydrogenases

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L-malate dehydrogenases
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L-malate dehydrogenases
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L-malate dehydrogenases
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L-malate dehydrogenases
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L-malate dehydrogenases
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L-malate dehydrogenases
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L-malate dehydrogenases
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L-malate dehydrogenases
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L-malate dehydrogenases
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L-malate dehydrogenases
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L-malate dehydrogenases
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L-malate: NAD oxidoreductase

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L-malate: NAD oxidoreductase
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L-malate: NAD oxidoreductase
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L-malate: NAD oxidoreductase
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L-malate: NAD+ oxidoreductase

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L-malate: NAD+ oxidoreductase
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L-malate: NAD+ oxidoreductase
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L-malate: NAD+ oxidoreductase
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L-malate: NAD+ oxidoreductase
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L-malate: NAD+ oxidoreductase
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L-malate: NAD+ oxidoreductase
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L-malate: NAD+ oxidoreductase
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L-malate:NAD oxidoreductase

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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-malate:NAD oxidoreductase
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L-MDH

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LDH-like malate dehydrogenase

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LDH-like malate dehydrogenase
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ldh0076

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LEUM_0076

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m-MDH

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malate dehydrogenase

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malate dehydrogenase 2

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MalDH

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MDH

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Mdh1

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MDH2

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Mdh3

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isoform
mitochondrial malate dehydrogenase

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mitochondrial malate dehydrogenase
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mitochondrial malate dehydrogenase
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mitochondrial malate dehydrogenase
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mitochondrial malate dehydrogenase
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mMDH

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mMDH
mitochondrial isoenzyme
mMDH
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mitochondrial isoenzyme
NAD+-dependent malate dehydrogenase

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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent malate dehydrogenase
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NAD+-dependent MDH

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NAD-dependent malate dehydrogenase

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NAD-dependent malate dehydrogenase
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NAD-dependent malate dehydrogenase
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NAD-dependent malate dehydrogenase
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NAD-dependent MalDH

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NAD-dependent MDH

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NAD-malate dehydrogenase

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NAD-malate dehydrogenase
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NAD-MDH

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Pcal_1699

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pdNAD-MDH

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plastidial NAD-dependent malate dehydrogenase

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plastidial NAD-dependent malate dehydrogenase
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s-MDH

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additional information

MDH belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases
additional information
MDH belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases
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(S)-malate + NAD+ = oxaloacetate + NADH + H+
(S)-malate + NAD+ = oxaloacetate + NADH + H+

also oxidizes some other 2-hydroxydicarboxylic acids
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(S)-malate + NAD+ = oxaloacetate + NADH + H+
an ordered bi-bi mechanism with coenzyme binding first followed by the binding of substrate is able to explain the kinetic data. The proposed mechanism is similar to, but not identical to, the mechanism determined for the cytoplasmic isoform, cMDH
(S)-malate + NAD+ = oxaloacetate + NADH + H+
an ordered bi-bi mechanism with coenzyme binding first followed by the binding of substrate is able to explain the kinetic data. The proposed mechanism is similar to, but not identical to, the mechanism determined for the mitochondrial isoform, mMDH
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