ExplorEnz: EC 1.1.1.37

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1.1.1.37

Accepted name:

(S)-malate dehydrogenase (NAD⁺, oxaloacetate-forming)

Reaction:

(S)-malate + NAD⁺ = oxaloacetate + NADH + H⁺

For diagram of the 3-hydroxypropanoate/4-hydroxybutanoate cycle and dicarboxylate/4-hydroxybutanoate cycle in archaea, click here, for diagram of the citric acid cycle, click here and for diagram of the glyoxylate cycle, click here

Other name(s):

malic dehydrogenase (ambiguous); L-malate dehydrogenase (ambiguous); NAD-L-malate dehydrogenase (ambiguous); malic acid dehydrogenase (ambiguous); NAD-dependent malic dehydrogenase (ambiguous); NAD-malate dehydrogenase (ambiguous); NAD-malic dehydrogenase (ambiguous); malate (NAD) dehydrogenase (ambiguous); NAD-dependent malate dehydrogenase (ambiguous); NAD-specific malate dehydrogenase (ambiguous); NAD-linked malate dehydrogenase (ambiguous); MDH (ambiguous); L-malate-NAD⁺ oxidoreductase (ambiguous); malate dehydrogenase (ambiguous); aromatic α-keto acid; KAR; 2-oxo acid reductase

Systematic name:

(S)-malate:NAD⁺ oxidoreductase

Comments:

There are several forms of malate dehydrogenases that differ in their use of substrates 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 and aromatic α-keto 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).

Links to other databases:

BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-64-3

References:

1.	Wolfe, R.G. and Nielands, J.B. Some molecular and kinetic properties of heart malic dehydrogenase. J. Biol. Chem. 221 (1956) 61–69. [PMID: 13345798]
2.	Guha, A., Englard, S. and Listowsky, I. Beef heart malic dehydrogenases. VII. Reactivity of sulfhydryl groups and conformation of the supernatant enzyme. J. Biol. Chem. 243 (1968) 609–615. [PMID: 5637713]
3.	McReynolds, M.S. and Kitto, G.B. Purification and properties of Drosophila malate dehydrogenases. Biochim. Biophys. Acta 198 (1970) 165–175. [DOI] [PMID: 4313528]
4.	Banaszak, L.J. and Bradshaw, R.A. Malate dehydrogenase. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 11, Academic Press, New York, 1975, pp. 369–396.
5.	Friedrich, C.A., Morizot, D.C., Siciliano, M.J. and Ferrell, R.E. The reduction of aromatic α-keto acids by cytoplasmic malate dehydrogenase and lactate dehydrogenase. Biochem. Genet. 25 (1987) 657–669. [DOI] [PMID: 2449162]
6.	Friedrich, C.A., Ferrell, R.E., Siciliano, M.J. and Kitto, G.B. Biochemical and genetic identity of α-keto acid reductase and cytoplasmic malate dehydrogenase from human erythrocytes. Ann. Hum. Genet. 52 (1988) 25–37. [DOI] [PMID: 3052244]

[EC 1.1.1.37 created 1961 (EC 1.1.1.96 created 1966, incorporated 2025), modified 2025]