The Enzyme Database

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EC 1.1.1.39     
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 1.1.1.38, which catalyses a similar reaction, this enzyme can not bind oxaloacetate, and thus does not decarboxylate exogeneously-added oxaloacetate. cf. EC 1.1.1.37, malate dehydrogenase; EC 1.1.1.38, malate dehydrogenase (oxaloacetate-decarboxylating); and EC 1.1.1.83, D-malate dehydrogenase (decarboxylating).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9028-46-0
References:
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 1.1.1.39 created 1961]
 
 


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