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Article

Mapping the substrate binding site of phenylacetone monooxygenase from Thermobifida fusca by mutational analysis.

Applied and environmental microbiology - 15 Aug 2011

Dudek Hanna M, de Gonzalo Gonzalo, Pazmiño Daniel E Torres, Stepniak Piotr, Wyrwicz Lucjan S, Rychlewski Leszek, Fraaije Marco W

Abstract excerpt

Baeyer-Villiger monooxygenases catalyze oxidations that are of interest for biocatalytic applications. Among these enzymes, phenylacetone monooxygenase (PAMO) from Thermobifida fusca is the only protein showing remarkable stability. While related enzymes often present a broad substrate scope, PAMO accepts only a limited number of substrates. Due to the absence of a substrate in the elucidated crystal structure of...

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PMID: 21724896
DOI: 10.1128/AEM.00687-11
PMCID: PMC3165276

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