Biochemical and structural characterization of the tautomycetin thioesterase: Analysis of a stereoselective polyketide hydrolase

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

doi:10.1002/anie.201000032

Biochemical and structural characterization of the tautomycetin thioesterase: Analysis of a stereoselective polyketide hydrolase

Jamie B. Scaglione, David L. Akey, Rachel Sullivan, Jeffrey D. Kittendorf, Christopher M. Rath, Eung Soo Kim, Janet L. Smith, David H. Sherman

University of Michigan, Ann Arbor

Research output: Contribution to journal › Article › peer-review

43 Scopus citations

Abstract

[Figure Presented] A narrow tunnel: Biochemical and structural analysis of the tautomycetin thioesterase (TE) has provided the first highresolution 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.

Original language	English
Pages (from-to)	5726-5730
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	49
Issue number	33
DOIs	https://doi.org/10.1002/anie.201000032
State	Published - 2 Aug 2010

Keywords

Acyltransferases
Polyketides
Structure elucidation
Tautomycetin
Thioesterases

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abstract = "[Figure Presented] A narrow tunnel: Biochemical and structural analysis of the tautomycetin thioesterase (TE) has provided the first highresolution 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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AU - Kittendorf, Jeffrey D.

AU - Rath, Christopher M.

AU - Kim, Eung Soo

AU - Smith, Janet L.

AU - Sherman, David H.

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AB - [Figure Presented] A narrow tunnel: Biochemical and structural analysis of the tautomycetin thioesterase (TE) has provided the first highresolution 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.

KW - Acyltransferases

KW - Polyketides

KW - Structure elucidation

KW - Tautomycetin

KW - Thioesterases

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Biochemical and structural characterization of the tautomycetin thioesterase: Analysis of a stereoselective polyketide hydrolase

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Keywords

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