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

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

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 macrolact...

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Veröffentlicht in:Angewandte Chemie (International ed.) 2010-08, Vol.49 (33), p.5726-5730
Hauptverfasser: Scaglione, Jamie B, Akey, David L, Sullivan, Rachel, Kittendorf, Jeffrey D, Rath, Christopher M, Kim, Eung-Soo, Smith, Janet L, Sherman, David H
Format: Artikel
Sprache:eng
Schlagworte:
acyltransferases
BASIC BIOLOGICAL SCIENCES
BIOSYNTHESIS
Catalytic Domain
ENZYMES
Furans - chemistry
GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
HYDROLASES
Hydrolysis
Lipids - biosynthesis
Lipids - chemistry
Polyketide Synthases - chemistry
Polyketide Synthases - metabolism
polyketides
Stereoisomerism
Streptomyces - enzymology
structure elucidation
SUBSTRATES
tautomycetin
thioesterases
Thiolester Hydrolases - chemistry
Thiolester Hydrolases - metabolism
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Beschreibung
Zusammenfassung: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201000032