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Malate dehydrogenase (oxaloacetate-decarboxylating)

Class of enzymes

Field	Value
Name	malate dehydrogenase (oxaloacetate-decarboxylating)
EC_number	1.1.1.38
CAS_number	9080-52-8
GO_code	0016619
image	1efk.jpg
caption	malic enzyme tetramer, Human

In enzymology, a malate dehydrogenase (oxaloacetate-decarboxylating) () is an enzyme that catalyzes the chemical reaction

The two substrates of this enzyme are (S)-malic acid and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are pyruvic acid, carbon dioxide, and reduced NADH.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (S)-malate:NAD+ oxidoreductase (oxaloacetate-decarboxylating). Other names in common use include malic enzyme, pyruvic-malic carboxylase, NAD+-specific malic enzyme, NAD+-malic enzyme, and NAD+-linked malic enzyme. This enzyme participates in pyruvate metabolism.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , and .

References

{{KEGG enzyme. 1.1.1.38
(1951). "Biosynthesis of dicarboxylic acids by carbon dioxide fixation. V Further studies of the "malic" enzyme of ''Lactobacillus arabinosus''". J. Biol. Chem..

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ec-1.1.1 nadh-dependent-enzymes enzymes-of-known-structure

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