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
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

 
 
 
H+
 
H+
 
+ CO2 + NADH
 

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.[1][2]

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

References

  1. ^ Enzyme 1.1.1.38 at KEGG Pathway Database.
  2. ^ 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 (1): 301–312. doi:10.1016/S0021-9258(18)55934-2. PMID 14917678.