Haynes, Stuart W., Sydor, Paulina K., Stanley, Anna E., Song, Lijiang and Challis, Gregory L.. (2008) Role and substrate specificity of the Streptomyces coelicolor RedH enzyme in undecylprodiginine biosynthesis. Chemical Communications (No.16). pp. 1865-1867. ISSN 1359-7345

Full text not available from this repository.

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.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QR Microbiology
Divisions:	Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH):	Streptomyces coelicolor, Enzymes, Catalysis, Antibiotics -- Synthesis, Antibiotic-producing organisms
Journal or Publication Title:	Chemical Communications
Publisher:	Royal Society of Chemistry
ISSN:	1359-7345
Date:	28 April 2008
Number:	No.16
Number of Pages:	3
Page Range:	pp. 1865-1867
Identification Number:	10.1039/b801677a
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), National Institutes of Health (U.S.) (NIH), European Union (EU)
Grant number:	BBSSK200310147 (BBSRC), GM077147 (NIH), 005224 (EU)
References:	1 A. Mortellaro, S. Songia, P. Gnocchi, M. Ferrari, C. Fornasiero, R. D’Alessio, A. Isetta, F. Colotta and J. Golay, J. Immunol., 1999, 162, 7102–7109. 2 N. N. Gerber, J. Antibiot., 1975, 28, 194–199; M. Isaka, A. Jaturapat, J. Kramyu, M. Tanticharoen and Y. Thebtaranonth, Antimicrob. Agents Chemother., 2002, 46, 1112–1113. 3 B. Montaner and R. Perez-Tomas, Curr. Cancer Drug Targets, 2003, 3, 57–65. 4 A. Fu¨ rtsner, Angew. Chem., Int. Ed., 2003, 42, 3582–3603. 5 G. C. Shore, J. Bajorath, F. L. Stahura and M. S. R. Murthy, International patent application WO 2003015788, 2003. 6 M. Nguyen, R. C. Marcellus, A. Roulston, M. Watson, L. Serfass, S. R. M. Madiraju, D. Goulet, J. Viallet, L. Belec, X. Billot, S. Acoca, E. Purisima, A. Wiegmans, L. Cluse, R. W. Johnstone, P. Beauparlant and G. C. Shore, Proc. Natl. Acad. Sci. U. S. A., 2007, 104, 19512–19517. 7 S.W. Tsao, B. A. Rudd, X. G. He, C. J. Chang and H. G. Floss, J. Antibiot., 1985, 38, 128–131. 8 S. J. Mo, P. K. Sydor, C. Corre, M. M. Alhamadsheh, A. E. Stanley, S. W. Haynes, L. Song, K. A. Reynolds and G. L. Challis, Chem. Biol., 2008, 15, 137–148. 9 A. M. Cerdeno, M. J. Bibb and G. L. Challis, Chem. Biol., 2001, 8, 211–224. 10 A. E. Stanley, L. J. Walton, M. Kourdi-Zerikly, C. Corre and G. L. Challis, Chem. Commun., 2006, 3981–3983. 11 M. G. Thomas, M. D. Burkart and C. T. Walsh, Chem. Biol., 2002, 9, 171–184. 12 S. Garneau-Tsodikova, P. C. Dorrestein, N. L. Kelleher and C. T. Walsh, J. Am. Chem. Soc., 2006, 128, 12600–12601. 13 N. R. Williamson, H. T. Simonsen, R. A. A. Ahmed, G. Goldet, H. Slater, L. Woodley, F. J. Leeper and G. P. C. Salmond, Mol. Microbiol., 2005, 56, 971–989. 14 B. Gust, G. L. Challis, K. Fowler, T. Kieser and K. F. Chater, Proc. Natl. Acad. Sci. U. S. A., 2003, 100, 1541–1546. 15 K. Dairi, S. Tripathy, G. Attardo and J.-F. Lavalle´ e, Tetrahedron Lett., 2006, 47, 2605–2606. 16 Y. Kayakawa, K. Kawakami, H. Seto and K. Furihata, Tetrahedron Lett., 1992, 33, 2701–2704. 17 H. H. Wasserman, G. C. Rodgers and D. D. Keith, Tetrahedron, 1976, 32, 1851–1854. 18 These results were first presented on 20 June 2007 at the Chemistry and Biology of Natural Products Biosynthesis III, University of Bristol, UK.
URI:	http://wrap.warwick.ac.uk/id/eprint/30277

Data sourced from Thomson Reuters' Web of Knowledge

Request changes to a record

Actions (login required)

View Item