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Issue 6, 2021
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A new clade of styrene monooxygenases for (R)-selective epoxidation

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Abstract

Styrene monooxygenases (SMOs) are excellent enzymes for the production of (S)-enantiopure epoxides, but so far, only one (R)-selective SMO has been identified with a narrow substrate spectrum. Mining the NCBI non-redundant protein sequences returned a new distinct clade of (R)-selective SMOs. Among them, SeStyA from Streptomyces exfoliatus, AaStyA from Amycolatopsis albispora, and PbStyA from Pseudonocardiaceae were carefully characterized and found to convert a spectrum of styrene analogues into the corresponding (R)-epoxides with up to >99% ee. Moreover, site 46 (AaStyA numbering) was identified as a critical residue that affects the enantioselectivity of SMOs. Phenylalanine at site 46 was required for the (R)-selective SMO to endow excellent enantioselectivity. The identification of new (R)-selective SMOs would add a valuable green alternative to the synthetic tool box for the synthesis of enantiopure (R)-epoxides.

Graphical abstract: A new clade of styrene monooxygenases for (R)-selective epoxidation

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Supplementary files

Article information


Submitted
01 Dec 2020
Accepted
16 Jan 2021
First published
18 Jan 2021

Catal. Sci. Technol., 2021,11, 2195-2201
Article type
Paper

A new clade of styrene monooxygenases for (R)-selective epoxidation

H. Xiao, S. Dong, Y. Liu, X. Pei, H. Lin and Z. Wu, Catal. Sci. Technol., 2021, 11, 2195
DOI: 10.1039/D0CY02312D

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