Malate dehydrogenase (oxaloacetate-decarboxylating)

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In enzymology, a malate dehydrogenase (oxaloacetate-decarboxylating) (EC 1.1.1.38) is an enzyme that catalyzes the chemical reaction

(S)-malate + NAD⁺ $\rightleftharpoons$ pyruvate + CO₂ + NADH

Thus, the two substrates of this enzyme are (S)-malate and NAD⁺, whereas its 3 products are pyruvate, CO₂, and 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1GZ3, 1LLQ, 1O0S, 1PJL, 1WW8, and 2DVM.

[edit] References

IUBMB entry for 1.1.1.38
BRENDA references for 1.1.1.38 (Recommended.)
PubMed references for 1.1.1.38
PubMed Central references for 1.1.1.38
Google Scholar references for 1.1.1.38
Kaufman S, Korkes S and del Campillo A (1951). "Biosynthesis of dicarboxylic acids by carbon dioxide fixation. V Further studies of the "malic" enzyme of Lactobacillus arabinosus". J. Biol. Chem. 192: 301–312.