Please use this identifier to cite or link to this item: https://doi.org/10.1002/anie.201001772
Title: High-throughput method for determining the enantioselectivity of enzyme-catalyzed hydroxylations based on mass spectrometry
Authors: Chen, Y. 
Tang, W.L.
Mou, J.
Li, Z. 
Keywords: Enantioselectivity
Enzyme catalysis
High-throughput screening
Hydroxylation
Mass spectrometry
Issue Date: 19-Jul-2010
Source: Chen, Y.,Tang, W.L.,Mou, J.,Li, Z. (2010-07-19). High-throughput method for determining the enantioselectivity of enzyme-catalyzed hydroxylations based on mass spectrometry. Angewandte Chemie - International Edition 49 (31) : 5278-5283. ScholarBank@NUS Repository. https://doi.org/10.1002/anie.201001772
Abstract: (Chemical equation presented) Up to speed: An accurate, sensitive, high-throughput, and simple method for measuring the product ee value of enzyme-catalyzed hydroxylations (see scheme) is based on the use of enantiopure or enantioenriched deuterated substrates and mass spectrometric detection. © 2010 Wiley-VCH Verlag GmbH & CO. KGaA.
Source Title: Angewandte Chemie - International Edition
URI: http://scholarbank.nus.edu.sg/handle/10635/64030
ISSN: 14337851
DOI: 10.1002/anie.201001772
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