Malate dehydrogenase (oxaloacetate-decarboxylating)

malate dehydrogenase (oxaloacetate-decarboxylating)
malic enzyme tetramer, Human
Identifiers
EC no.	1.1.1.38
CAS no.	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  / QuickGO
Search PMC articles PubMed articles NCBI proteins

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

(S)-malate + NAD⁺ ${\displaystyle \rightleftharpoons }$ 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.

Structural studies

As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1DO8, 1EFK, 1EFL, 1GZ3, 1LLQ, 1O0S, 1PJ2, 1PJ3, 1PJ4, 1PJL, 1QR6, 1WW8, and 2DVM.

See also

• ME2 (gene)

References

• Kaufman S, Korkes S, 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. PMID 14917678.

This page was last edited on 6 May 2024, at 15:27