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
Citation: 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
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

37
checked on Jul 10, 2018

WEB OF SCIENCETM
Citations

27
checked on May 30, 2018

Page view(s)

50
checked on Apr 21, 2018

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.