Lactate—malate transhydrogenase
In this article we are going to talk about Lactate—malate transhydrogenase, a topic of great relevance today. Lactate—malate transhydrogenase is a complex issue that covers different aspects that affect society as a whole. From its impact on the economy to its influence on personal relationships, Lactate—malate transhydrogenase is an issue that leaves no one indifferent. Throughout this article we will explore the different approaches and perspectives that exist around Lactate—malate transhydrogenase, with the aim of offering a more complete and in-depth understanding of this very relevant topic.
| lactate—malate transhydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.1.99.7 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
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.
