| Literature DB >> 24157359 |
Dirk Tischler1, Michael Schlömann, Willem J H van Berkel, George T Gassner.
Abstract
StyA2B represents a new class of styrene monooxygenases that integrates flavin-reductase and styrene-epoxidase activities into a single polypeptide. This naturally-occurring fusion protein offers new avenues for studying and engineering biotechnologically relevant enantioselective biochemical epoxidation reactions. Stopped-flow kinetic studies of StyA2B reported here identify reaction intermediates similar to those reported for the separate reductase and epoxidase components of related two-component systems. Our studies identify substrate epoxidation and elimination of water from the FAD C(4a)-hydroxide as rate-limiting steps in the styrene epoxidation reaction. Efforts directed at accelerating these reaction steps are expected to greatly increase catalytic efficiency and the value of StyA2B as biocatalyst.Entities:
Keywords: Catalytic mechanism; FAD (C4a)-hydroperoxide and FAD C(4a)-hydroxide; FAD(ox) and FAD(red); FADH(OOH) and FADH(OH); Flavoprotein; Monooxygenase; Rhodococcus opacus 1CP; SMO; StyA and StyB; StyA2B; Styrene epoxidation; epoxidase and reductase subunit of conventional two-component SMOs; naturally fused self-sufficient SMO comprising reductase (B) and epoxidase (A2); oxidized and reduced FAD; styrene monooxygenase
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Year: 2013 PMID： 24157359 PMCID： PMC3858207 DOI： 10.1016/j.febslet.2013.10.013
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124