Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom?

Chemical Communications Pub Date: 2012-03-05 DOI: 10.1039/C2CC30779K

Abstract

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.

Graphical abstract: Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom
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