Journal
BIOTECHNOLOGY LETTERS
Volume 33, Issue 3, Pages 611-616Publisher
SPRINGER
DOI: 10.1007/s10529-010-0472-9
Keywords
Biocatalysis; Protein engineering; Rational design; Styrene monooxygenase; Substrate preference
Categories
Funding
- National Natural Science Foundation of China [20802073]
- Chinese Academy of Sciences [KSCX2-YW-G-075]
- Sichuan Province Science Foundation for Young Scholars [08ZQ026-023]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available