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

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

doi:10.1039/b801677a

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

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

Research output: Contribution to journal › Article › Research › peer-review

39 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1865-1867
Number of pages	3
Journal	Chemical Communications
Issue number	16
DOIs	https://doi.org/10.1039/b801677a
Publication status	Published - 14 Apr 2008
Externally published	Yes

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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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AU - Haynes, Stuart W.

AU - Sydor, Paulina K.

AU - Stanley, Anna E.

AU - Song, Lijiang

AU - Challis, Gregory L.

PY - 2008/4/14

Y1 - 2008/4/14

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AB - 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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JO - Chemical Communications

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

Abstract

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