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Rapid Determination of Both the Activity and Enantioselectivity of Ketoreductases
Author(s) -
Truppo Matthew D.,
Escalettes Franck,
Turner Nicholas J.
Publication year - 2008
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200705046
Subject(s) - abts , horseradish peroxidase , enantioselective synthesis , substrate (aquarium) , chemistry , peroxidase , oxidase test , enzyme , chromatography , enzyme assay , combinatorial chemistry , biochemistry , catalysis , dpph , antioxidant , biology , ecology
Fast and furious : A rapid and inexpensive assay for determining both the activity and enantioselectivity of ketoreductases (KREDs) has been developed (see scheme; HRP=horseradish peroxidase, ABTS=2,2′‐azino‐di(3‐ethyl benzthiazoline‐6‐sulfonic acid). This assay, which employs an enantioselective alcohol oxidase as a reporter enzyme, was used to screen a panel of 17 KREDs in only 10 min using less than 0.5 mg substrate.