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|Title:||Evolving P450pyr hydroxylase for highly enantioselective hydroxylation at non-activated carbon atom|
|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|
|Appears in Collections:||Staff Publications|
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