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.