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Activity of Lipases and Esterases towards Tertiary Alcohols: Insights into Structure–Function Relationships
Author(s) -
Henke Erik,
Pleiss Jürgen,
Bornscheuer Uwe T.
Publication year - 2002
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 - 10.1002/1521-3773(20020902)41:17<3211::aid-anie3211>3.0.co;2-u
Subject(s) - motif (music) , structural motif , chemistry , protein tertiary structure , sequence motif , enzyme , organic chemistry , stereochemistry , biochemistry , gene , physics , acoustics
A single amino acid pattern (GGG(A)X motif) in hydrolases controls their activity towards tertiary alcohols. Consequently, a range of active lipases and esterases which catalyze the efficient conversion of acetates of different tertiary alcohols (see scheme) and thereby facilitate access to this class of building blocks for organic synthesis, flavors, and fragrances was identified by sequence comparison. Hydrolases bearing an alternative GX motif were inactive.