Lactate 2-monooxygenase

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In enzymology, a lactate 2-monooxygenase (EC 1.13.12.4) is an enzyme that catalyzes the chemical reaction

(S)-lactate + O₂ $\rightleftharpoons$ 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2DU2.

[edit] References

IUBMB entry for 1.13.12.4
BRENDA references for 1.13.12.4 (Recommended.)
PubMed references for 1.13.12.4
PubMed Central references for 1.13.12.4
Google Scholar references for 1.13.12.4
Hayaishi O and Sutton WB (1957). "Enzymatic oxygen fixation into acetate concomitant with the enzymatic decarboxylation of L-lactate". J. Am. Chem. Soc. 79: 4809–4810. doi:10.1021/ja01574a060.
SUTTON WB (1957). "Mechanism of action and crystallization of lactic oxidative decarboxylase from Mycobacterium phlei". J. Biol. Chem. 226: 395–405. PMID 13428772.