4.7 Article

Role and substrate specificity of the Streptomyces coelicolor RedH enzyme in undecylprodiginine biosynthesis

Journal

CHEMICAL COMMUNICATIONS
Volume -, Issue 16, Pages 1865-1867

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/b801677a

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Funding

  1. Biotechnology and Biological Sciences Research Council [BBSSK200310147] Funding Source: Medline
  2. NIGMS NIH HHS [GM077147] Funding Source: Medline

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The function of RedH from Streptomyces coelicolor as an enzyme that catalyses the condensation of 4-methoxy- 2,2'- bipyrrole-5- carboxaldehyde (MBC) and 2-undecylpyrrole to form the natural product undecylprodiginine has been experimentally proven, and the substrate specificity of RedH has been probed in vivo by examining its ability to condense chemically-synthesised MBC analogues with 2-undecylpyrrole to afford undecylprodiginine analogues.

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