1246182-93-3Relevant academic research and scientific papers
Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom
Pham, Son Quang,Pompidor, Guillaume,Liu, Ji,Li, Xiao-Dan,Li, Zhi
supporting information; experimental part, p. 4618 - 4620 (2012/06/05)
Directed evolution of a monooxygenase to achieve very high enantioselectivity for hydroxylation at non-activated carbon atoms is demonstrated for the first time, where a triple mutant of P450pyr hydroxylase is obtained via determination of enzyme structure, iterative saturation mutagenesis, and high-throughput screening with a MS-based ee assay to increase the product ee from 53% to 98% for the hydroxylation of N-benzyl pyrrolidine to (S)-N-benzyl 3-hydroxypyrrolidine. The Royal Society of Chemistry 2012.
