title: Rational design of styrene monooxygenase mutants with altered substrate preference.
abstract: Styrene monooxygenase catalyzes the enantioselective epoxidation of styrene but displays significantly decreased activity toward styrene derivatives with an α- or β-substituent. Based on the X-ray crystal structure of the oxygenase subunit of styrene monooxygenase, molecular docking of α-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 α-ethylstyrene.
authors.affiliation: Chengdu Institute of Biology, Chinese Academy of Sciences, P.O. Box 416, Chengdu, 610041, China.
authors.forename: Abeer Ahmed
authors.initials: AA
authors.lastname: Qaed
authors.forename: Hui
authors.initials: H
authors.lastname: Lin
authors.forename: De-Fang
authors.initials: DF
authors.lastname: Tang
authors.forename: Zhong-Liu
authors.initials: ZL
authors.lastname: Wu
mesh_terms: D018360:Crystallography, X-Ray; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D010105:Oxygenases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015202:Protein Engineering / Q000379:methods*; D013379:Substrate Specificity / Q000235:genetics
chemical_list: D010105:Oxygenases; C026721:styrene monooxygenase