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Issue 16, 2008
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Role and substrate specificity of the Streptomyces coelicolor RedH enzyme in undecylprodiginine biosynthesis

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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.

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

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Publication details

The article was received on 30 Jan 2008, accepted on 03 Mar 2008 and first published on 14 Mar 2008


Article type: Communication
DOI: 10.1039/B801677A
Citation: Chem. Commun., 2008,0, 1865-1867

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

    S. W. Haynes, P. K. Sydor, A. E. Stanley, L. Song and G. L. Challis, Chem. Commun., 2008, 0, 1865
    DOI: 10.1039/B801677A

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