Activity of Lipases and Esterases towards Tertiary Alcohols: Insights into Structure-Function Relationships

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 cla...

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Published inAngewandte Chemie (International ed.) Vol. 41; no. 17; pp. 3211 - 3213
Main Authors Henke, Erik, Pleiss, Jürgen, Bornscheuer, Uwe T
Format Journal Article
LanguageEnglish
Published Weinheim Wiley-VCH Verlag 02.09.2002
WILEY-VCH Verlag
WILEY‐VCH Verlag
Subjects
Acetates - chemistry
Acetylcholinesterase - chemistry
Alcohols - chemistry
Animals
biotransformation
Bungarus
Candida - enzymology
Electrophorus
enzyme catalysis
esterases
Esterases - chemistry
Humans
Hydrolases - chemistry
Lipase - chemistry
lipases
molecular modeling
Protein Conformation
Structure-Activity Relationship
tertiary alcohols
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Summary: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.
Bibliography:http://dx.doi.org/10.1002/1521-3773(20020902)41:17<3211::AID-ANIE3211>3.0.CO;2-U
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ArticleID:ANIE3211
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We thank Prof. R. D. Schmid (Institute of Technical Biochemistry (ITB), Stuttgart University) for helpful discussions and Sandra Vorlová (ITB) for providing recombinant hAChE and bAChE. This work was financed by the German Research Foundation (DFG, Bonn (Germany), Grant Bo 1475/2-1).
We thank Prof. R. D. Schmid (Institute of Technical Biochemistry (ITB), Stuttgart University) for helpful discussions and Sandra Vorlová (ITB) for providing recombinant hAChE and bAChE. This work was financed by the German Research Foundation (DFG, Bonn (Germany), Grant Bo 1475/2‐1).
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ISSN:1433-7851
1521-3773
DOI:10.1002/1521-3773(20020902)41:17<3211::AID-ANIE3211>3.0.CO;2-U