Metamorphic enzyme assembly in polyketide diversification

Liangcai Gu, Bo Wang, Amol Kulkarni, Todd W. Geders, Rashel V. Grindberg, Lena Gerwick, Kristina Håkansson, Peter Wipf, Janet L. Smith, William H. Gerwick and David H. Sherman ()
Additional contact information
Liangcai Gu: Life Sciences Institute,
Bo Wang: Department of Chemistry,
Amol Kulkarni: University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA
Todd W. Geders: Life Sciences Institute,
Rashel V. Grindberg: Scripps Institution of Oceanography & Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, California 92093, USA
Lena Gerwick: Scripps Institution of Oceanography & Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, California 92093, USA
Kristina Håkansson: Department of Chemistry,
Peter Wipf: University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA
Janet L. Smith: Life Sciences Institute,
William H. Gerwick: Scripps Institution of Oceanography & Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California at San Diego, La Jolla, California 92093, USA
David H. Sherman: Life Sciences Institute,

Nature, 2009, vol. 459, issue 7247, 731-735

Abstract: Cyclopropane and vinyl chloride share biosynthesis resources A study of the pathways responsible for the synthesis of two natural products — curacin and jamaicamide — in the cyanobacterium Lyngbya majuscula reveals two biosynthetic pathways with high sequence identity. Yet they are responsible for the production of two dramatically different chemical motifs: a β-branched cyclopropane in the curacin A pathway, and a vinyl chloride group in the jamaicamide pathway. The biochemical characterization of several domains of the biosynthetic pathways, including the halogenase domains and the enoyl reductase domains, reveals details of the mechanisms by which the cyclopropane and vinyl chloride groups are generated.

Date: 2009
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DOI: 10.1038/nature07870

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