Please use this identifier to cite or link to this item: https://doi.org/10.1039/c2cc30779k
Title: Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom
Authors: Pham, S.Q.
Pompidor, G.
Liu, J.
Li, X.-D.
Li, Z. 
Issue Date: 14-May-2012
Source: Pham, S.Q., Pompidor, G., Liu, J., Li, X.-D., Li, Z. (2012-05-14). Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom. Chemical Communications 48 (38) : 4618-4620. ScholarBank@NUS Repository. https://doi.org/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. This journal is © The Royal Society of Chemistry 2012.
Source Title: Chemical Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/63883
ISSN: 13597345
DOI: 10.1039/c2cc30779k
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