Lactate—malate transhydrogenase

In enzymology, a lactate—malate transhydrogenase (EC 1.1.99.7) is an enzyme that catalyzes the chemical reaction

(S)-lactate + oxaloacetate pyruvate + malate
lactate—malate transhydrogenase
Identifiers
EC no.1.1.99.7
CAS no.9077-15-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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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