Lactate—malate transhydrogenase
| lactate—malate transhydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.1.99.7 | ||||||||
| CAS number | 9077-15-0 | ||||||||
| 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 | ||||||||
| |||||||||
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.
References
Further reading
- Allen SH (1966). "The isolation and characterization of malate-lactate transhydrogenase from Micrococcus lactilyticus". J. Biol. Chem. 241 (22): 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 (3): 909–16. PMID 4333516.
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