Issue 16, 2008
From the journal:

Chemical Communications

Chemoenzymatic synthesis of prodigiosin analogues—exploring the substrate specificity of PigC†

Suresh R. Chawrai,a   Neil R. Williamson,b   George P. C. Salmond*b  and  Finian J. Leeper*a  

* Corresponding authors

a University of Cambridge, Department of Chemistry, Lensfield Road, Cambridge, UK
E-mail: fjl1@cam.ac.uk
Fax: +44 1223 336362
Tel: +44 1223 336403

b University of Cambridge, Department of Biochemistry, Tennis Court Road, Cambridge, UK
E-mail: gpcs@mole.bio.cam.ac.uk
Fax: +44 1223 766108
Tel: +44 1223 333650

Abstract

Analogues of prodigiosin, a tripyrrolic pigment produced by Serratia species with potent immunosuppressive and anticancer activities, have been produced by feeding synthetic analogues of the normal precursor MBC to mutants of Serratia sp. ATCC 39006 or to engineered strains of Escherichia coli; in this way it has been shown that the prodigiosin synthesising enzyme, PigC, has a relaxed substrate-specificity.

Graphical abstract: Chemoenzymatic synthesis of prodigiosin analogues—exploring the substrate specificity of PigC

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Article information

DOI
https://doi.org/10.1039/B719353J
Article type
Communication
Submitted
14 Dec 2007
Accepted
15 Jan 2008
First published
05 Feb 2008

Chem. Commun., 2008, 1862-1864

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Chemoenzymatic synthesis of prodigiosin analogues—exploring the substrate specificity of PigC

S. R. Chawrai, N. R. Williamson, G. P. C. Salmond and F. J. Leeper, Chem. Commun., 2008, 1862 DOI: 10.1039/B719353J

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