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

Literature Information

Publication Date 2008-03-14
DOI 10.1039/B801677A
Impact Factor 6.222
Authors

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


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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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