Biochemical and Structural Characterization of the Tautomycetin Thioesterase: Analysis of a Stereoselective Polyketide Hydrolase | Zendy

Scaglione Jamie B. | Zendy; Akey David L. | Zendy; Sullivan Rachel | Zendy; Kittendorf Jeffrey D. | Zendy; Rath Christopher M. | Zendy; Kim EungSoo | Zendy; Smith Janet L. | Zendy; Sherman David H. | Zendy

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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.

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