Elucidation of the Cryptic Epimerase Activity of Redox-Inactive Ketoreductase Domains from Modular Polyketide Synthases by Tandem Equilibrium Isotope Exchange-Reference-Cited by-同舟云学术

Elucidation of the Cryptic Epimerase Activity of Redox-Inactive Ketoreductase Domains from Modular Polyketide Synthases by Tandem Equilibrium Isotope Exchange

Published:2014-07-10 Issue:29 Volume:136 Page:10190-10193
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Garg Ashish¹,Xie Xinqiang¹,Keatinge-Clay Adrian²,Khosla Chaitan³,Cane David E.¹

Affiliation:

1. Department of Chemistry, Box H, Brown University, Providence, Rhode Island 02912-9108, United States

2. Department of Chemistry and Biochemistry, the University of Texas at Austin, 1 University Station A5300, Austin, Texas 78712-0165, United States

3. Departments of Chemical Engineering, Chemistry, and Biochemistry, Stanford University, Stanford, California 94305, United States

Funder

Welch Foundation

National Institutes of Health

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja5056998

Reference19 articles.

1. The Structure of a Ketoreductase Determines the Organization of the β-Carbon Processing Enzymes of Modular Polyketide Synthases

2. A Tylosin Ketoreductase Reveals How Chirality Is Determined in Polyketides

3. Structural and Functional Analysis of A-Type Ketoreductases from the Amphotericin Modular Polyketide Synthase

4. Structural and Functional Analysis of C2-Type Ketoreductases from Modular Polyketide Synthases

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