Article
Mutations at the putative active cavity of styrene monooxygenase: enhanced activity and reversed enantioselectivity.
Journal of biotechnology - 31 Oct 2012
Lin Hui, Tang De-Fang, Ahmed Abeer Ahmed Qaed, Liu Yan, Wu Zhong-Liu
Abstract excerpt
Styrene monooxygenase (SMO) catalyzes the first step of styrene degradation, and also serves as an important enzyme for the synthesis of enantiopure epoxides. To enhance its activity, molecular docking of styrene was performed based on the X-ray crystal structure of the oxygenase subunit of SMO to identify three amino acid residues (Tyr73, His76 and Ser96) being adjacent to the phenyl ring of styrene. Variants at...
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