Lactate-malate transhydrogenase
From Wikipedia, the free encyclopedia
In enzymology, a lactate---malate transhydrogenase (EC 1.1.99.7) is an enzyme that catalyzes the chemical reaction
- (S)-lactate + oxaloacetate pyruvate + malate
Thus, the two substrates of this enzyme are (S)-lactate and oxaloacetate, whereas its two products are pyruvate and malate.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with other acceptors. The systematic name of this enzyme class is (S)-lactate:oxaloacetate oxidoreductase. This enzyme is also called malate-lactate transhydrogenase. This enzyme participates in pyruvate metabolism. It employs one cofactor, nicotinamide D-ribonucleotide.
[edit] References
- IUBMB entry for 1.1.99.7
- BRENDA references for 1.1.99.7 (Recommended.)
- PubMed references for 1.1.99.7
- PubMed Central references for 1.1.99.7
- Google Scholar references for 1.1.99.7
- Allen SH (1966). "The isolation and characterization of malate-lactate transhydrogenase from Micrococcus lactilyticus". J. Biol. Chem. 241: 5266–75. PMID 4289051.
- Allen SH, Patil JR (1972). "Studies on the structure and mechanism of action of the malate-lactate transhydrogenase". J. Biol. Chem. 247: 909–16. PMID 4333516.
[edit] External links
-
- The CAS registry number for this enzyme class is 9077-15-0.