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Biochemical and Structural Characterization of the Tautomycetin Thioesterase: Analysis of a Stereoselective Polyketide Hydrolase
Author(s) -
Scaglione Jamie B.,
Akey David L.,
Sullivan Rachel,
Kittendorf Jeffrey D.,
Rath Christopher M.,
Kim EungSoo,
Smith Janet L.,
Sherman David H.
Publication year - 2010
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.201000032
Subject(s) - thioesterase , polyketide , stereochemistry , stereoselectivity , biosynthesis , enzyme , hydrolase , chemistry , computational biology , biochemistry , biology , catalysis
A narrow tunnel : Biochemical and structural analysis of the tautomycetin thioesterase (TE) has provided the first high‐resolution structure of a linear‐chain‐terminating TE in polyketide biosynthesis, showing the enzyme to be stereoselective with a constrained substrate chamber relative to macrolactone‐forming thioesterases.