期刊
BIOTECHNOLOGY LETTERS
卷 33, 期 3, 页码 611-616出版社
SPRINGER
DOI: 10.1007/s10529-010-0472-9
关键词
Biocatalysis; Protein engineering; Rational design; Styrene monooxygenase; Substrate preference
资金
- National Natural Science Foundation of China [20802073]
- Chinese Academy of Sciences [KSCX2-YW-G-075]
- Sichuan Province Science Foundation for Young Scholars [08ZQ026-023]
Styrene monooxygenase catalyzes the enantioselective epoxidation of styrene but displays significantly decreased activity toward styrene derivatives with an alpha- or beta-substituent. Based on the X-ray crystal structure of the oxygenase subunit of styrene monooxygenase, molecular docking of alpha-ethylstyrene was performed to identify adjacent residues. Four amino acid substitutions (R43A, L44A, L45A, and N46A) were introduced into the enzyme by site-directed mutagenesis. All four mutations led to a change of substrate preference. The mutant L45A, in particular, exhibited an altered substrate preference toward the bulkier substrate alpha-ethylstyrene.
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