Malate dehydrogenase (oxaloacetate-decarboxylating)
| malate dehydrogenase (oxaloacetate-decarboxylating) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.1.1.38 | ||||||||
| CAS number | 9080-52-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
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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+
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.
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.
See also
References
- 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.
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