Lactate 2-monooxygenase

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

(S)-lactate + O₂ ${\displaystyle \rightleftharpoons }$ 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.

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): 4809–4810. doi:10.1021/ja01574a060.
• Sutton WB (May 1957). "Mechanism of action and crystallization of lactic oxidative decarboxylase from Mycobacterium phlei". The Journal of Biological Chemistry. 226 (1): 395–405. PMID 13428772.

This page was last edited on 26 August 2023, at 14:42