Functional characterization of an (R)-selective styrene monooxygenase from streptomyces sp. NRRL S-31.
Enzyme Microb Technol
; 132: 109391, 2020 Jan.
Article
em En
| MEDLINE
| ID: mdl-31731956
ABSTRACT
Styrene monooxygenases (SMOs) are two-component enzymes known to catalyze the epoxidation of styrene to (S)-styrene oxide. In this work, we identified a new oxygenase component, named StStyA, from the genome of Streptomyces sp. NRRL S-31. StStyA displayed complementary stereoselectivity to all of the known SMOs when coupled with a known reductase component (PsStyB), which made it the first natural SMO that produces (R)-styrene oxide. Accordingly, a plasmid co-expressing StStyA and PsStyB was constructed, which led to an artificial two-component SMO, named StStyA/B. When applied in the bio-epoxidation of nine aromatic alkenes, the enzyme showed activity toward five alkenes, and consistently displayed (R)-selectivity. Excellent stereoselectivity was achieved for all five substrates with enantiomeric excesses ranging from 91% to >99%ee.
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MEDLINE
Assunto principal:
Oxigenases
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Streptomyces
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Proteínas de Bactérias
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article