Stereospecificity of the Dehydratase Domain of the Erythromycin Polyketide Synthase-Reference-Cited by-同舟云学术

Stereospecificity of the Dehydratase Domain of the Erythromycin Polyketide Synthase

Published:2010-10-06 Issue:42 Volume:132 Page:14697-14699
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Valenzano Chiara R.¹,You Young-Ok¹,Garg Ashish¹,Keatinge-Clay Adrian¹,Khosla Chaitan¹,Cane David E.¹

Affiliation:

1. Department of Chemistry, Box H, Brown University, Providence, Rhode Island 02912-9108, Departments of Chemical Engineering, Chemistry, and Biochemistry, Stanford University, Stanford, California 94305, and Department of Chemistry and Biochemistry, The University of Texas at Austin, 1 University Station A5300, Austin, Texas 78712-0165

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja107344h

Reference30 articles.

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2. Modular organization of genes required for complex polyketide biosynthesis

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4. An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea

5. Each PKS module typically has three core catalytic domains: the β-ketoacyl-ACP synthase (KS), the acyltransferase (AT), and the acyl carrier protein (ACP). Most modules also carry specific combinations of ketoreductase (KR), dehydratase (DH), and enoylreductase (ER) tailoring domains.

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