Phenylacetone monooxygenase

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In enzymology, a phenylacetone monooxygenase (EC 1.14.13.92) is an enzyme that catalyzes the chemical reaction

phenylacetone + NADPH + H⁺ + O₂ $\rightleftharpoons$ benzyl acetate + NADP⁺ + H₂O

The 4 substrates of this enzyme are phenylacetone, NADPH, H⁺, and O₂, whereas its 3 products are benzyl acetate, NADP⁺, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with NADH or NADPH as one donor, and incorporation of one atom o oxygen into the other donor. The systematic name of this enzyme class is phenylacetone,NADPH:oxygen oxidoreductase. This enzyme is also called PAMO.

[edit] References

IUBMB entry for 1.14.13.92
BRENDA references for 1.14.13.92 (Recommended.)
PubMed references for 1.14.13.92
PubMed Central references for 1.14.13.92
Google Scholar references for 1.14.13.92
Malito E, Alfieri A, Fraaije MW, Mattevi A (2004). "Crystal structure of a Baeyer-Villiger monooxygenase". Proc. Natl. Acad. Sci. U. S. A. 101: 13157–62. PMID 15328411.
DB (2005). "Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining". Appl. Microbiol. Biotechnol. 66: 393–400. PMID 15599520.