Lactate 2-monooxygenase
| lactate 2-monooxygenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.13.12.4 | ||||||||
| CAS number | 9028-72-2 | ||||||||
| 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 2-monooxygenase (EC 1.13.12.4) is an enzyme that catalyzes the chemical reaction
- (S)-lactate + O2 acetate + CO2 + H2O
Thus, the two substrates of this enzyme are (S)-lactate and O2, whereas its 3 products are acetate, CO2, and H2O.
This enzyme belongs to the family of oxidoreductases, specifically those acting on single donors with O2 as oxidant and incorporation of two atoms of oxygen into the substrate (oxygenases). The oxygen incorporated need not be derived from O with incorporation of one atom of oxygen (internal monooxygenases o internal mixed-function oxidases). The systematic name of this enzyme class is (S)-lactate:oxygen 2-oxidoreductase (decarboxylating). Other names in common use include lactate oxidative decarboxylase, lactate oxidase, lactic oxygenase, lactate oxygenase, lactic oxidase, L-lactate monooxygenase, lactate monooxygenase, and L-lactate-2-monooxygenase. This enzyme participates in pyruvate metabolism. It employs one cofactor, FMN.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2DU2.
References
- Hayaishi O; Sutton WB (1957). "Enzymatic oxygen fixation into acetate concomitant with the enzymatic decarboxylation of L-lactate". J. Am. Chem. Soc. 79 (17): 4809&ndash, 4810. doi:10.1021/ja01574a060.
- SUTTON WB (1957). "Mechanism of action and crystallization of lactic oxidative decarboxylase from Mycobacterium phlei". J. Biol. Chem. 226 (1): 395&ndash, 405. PMID 13428772.