1.
Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom.
Chem Commun (Camb)
; 48(38): 4618-20, 2012 May 14.
Artigo
em Inglês
| MEDLINE
| ID: mdl-22430002
RESUMO
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.