Please use this identifier to cite or link to this item:
|Title:||High-throughput method for determining the enantioselectivity of enzyme-catalyzed hydroxylations based on mass spectrometry|
|Authors:||Chen, Y. |
|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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Dec 12, 2017
checked on Dec 15, 2017
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.