The Enzyme Database

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Accepted name: malate dehydrogenase (decarboxylating)
Reaction: (S)-malate + NAD+ = pyruvate + CO2 + NADH
Other name(s): ’malic’ enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); NAD-specific malic enzyme (ambiguous); NAD-malic enzyme (ambiguous); malate dehydrogenase (decarboxylating) (ambiguous)
Systematic name: (S)-malate:NAD+ oxidoreductase (decarboxylating)
Comments: There are several forms of malate dehydrogenases that differ in their use of substrates and cofactors. This particular form is found only in the plant kingdom. Unlike EC, which catalyses a similar reaction, this enzyme can not bind oxaloacetate, and thus does not decarboxylate exogeneously-added oxaloacetate. cf. EC, malate dehydrogenase; EC, malate dehydrogenase (oxaloacetate-decarboxylating); and EC, D-malate dehydrogenase (decarboxylating).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-46-0
1.  Macrae, A.R. Isolation and properties of a ’malic’ enzyme from cauliflower bud mitochondria. Biochem. J. 122 (1971) 495–501. [PMID: 4399380]
2.  Grover, S.D., Canellas, P.F. and Wedding, R.T. Purification of NAD malic enzyme from potato and investigation of some physical and kinetic properties. Arch. Biochem. Biophys. 209 (1981) 396–407. [PMID: 7294802]
3.  Wedding, R.T. and Black, M.K. Physical and kinetic properties and regulation of the NAD malic enzyme purified from leaves of Crassula argentea. Plant Physiol. 72 (1983) 1021–1028. [PMID: 16663114]
4.  Wedding, R.T. Malic enzymes of higher plants: characteristics, regulation, and physiological function. Plant Physiol. 90 (1989) 367–371. [PMID: 16666776]
[EC created 1961]

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