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

ABSTRACT: 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 PAMO, the substrate binding site of this protein has not yet been defined. In this study, a structural model of cyclopentanone monooxygenase, which acts on a broad range of compounds, has been prepared and compared with the structure of PAMO. This revealed 15 amino acid positions in the active site of PAMO that may account for its relatively narrow substrate specificity. We design

SUBMITTER: Dudek HM 

PROVIDER: S-EPMC3165276 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature