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. 2008 Apr 28:(16):1865-7.
doi: 10.1039/b801677a. Epub 2008 Mar 14.

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

Stuart W Haynes  1 , Paulina K Sydor, Anna E Stanley, Lijiang Song, Gregory L Challis
Affiliations

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

Stuart W Haynes et al. Chem Commun (Camb). .

Abstract

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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