The Library
Petrobactin biosynthesis: AsbB catalyzes condensation of spermidine with N-8-citryl-spermidine and its N-1-(3,4-dihydroxybenzoyl) derivative
Tools
Tools
Tools
Oves-Costales, Daniel, Kadi, Nadia, Fogg, Mark J., Song, Lijiang, Wilson, Keith S. and Challis, Gregory L.. (2008) Petrobactin biosynthesis: AsbB catalyzes condensation of spermidine with N-8-citryl-spermidine and its N-1-(3,4-dihydroxybenzoyl) derivative. Chemical Communications (No.34). pp. 4034-4036. ISSN 1359-7345
Full text not available from this repository.
Official URL: http://dx.doi.org/10.1039/b809353a
Abstract
The AsbB enzyme, which is involved in the biosynthesis of the virulence-conferring siderophore petrobactin in Bacillus anthracis, is shown to catalyze efficient ATP-dependent condensation of spermidine, but not N-1-(3,4-dihydroxbenzoyl)-spermidine, with N-8-citryl-spermidine or N-1-(3,4-dihydroxbenzoyl)-N-8-citryl-spermidine, suggesting that N-1-(3,4-dihydroxbenzoyl)-spermidine is very unlikely to be a significant intermediate in petrobactin biosynthesis, contrary to previous suggestions.
| Item Type: | Journal Article |
|---|---|
| Subjects: | Q Science > QD Chemistry |
| Divisions: | Faculty of Science > Chemistry |
| Library of Congress Subject Headings (LCSH): | Siderophores -- Synthesis, Siderophores -- Therapeutic use, Spermidine |
| Journal or Publication Title: | Chemical Communications |
| Publisher: | Royal Society of Chemistry |
| ISSN: | 1359-7345 |
| Date: | 14 September 2008 |
| Number: | No.34 |
| Number of Pages: | 3 |
| Page Range: | pp. 4034-4036 |
| Identification Number: | 10.1039/b809353a |
| 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) |
| Grant number: | BB/FO13760/1 (BBSRC) |
| References: | 1 U. E. Schaible and S. H. E. Kaufmann, Nat. Rev. Microbiol., 2004, 2, 946–953. 2 J. H. Crosa and C. T. Walsh, Microbiol. Mol. Biol. Rev., 2002, 66, 223–249. 3 G. L. Challis, ChemBioChem, 2005, 6, 601–611. 4 F. Barona-Gomez, U. Wong, A. Giannakopulos, P. J. Derrick and G. L. Challis, J. Am. Chem. Soc., 2004, 126, 16282–16283. 5 D. Oves-Costales, N. Kadi, M. J. Fogg, L. Song, K. S. Wilson and G. L. Challis, J. Am. Chem. Soc., 2007, 129, 8416–8417. 6 N. Kadi, D. Oves-Costales, F. Barona-Gomez and G. L. Challis, Nat. Chem. Biol., 2007, 3, 652–656. 7 (a) M. Marcus and M. A. Marahiel, Microbiol. Mol. Biol. Rev., 2007, 71, 413–451; (b) R. R.Monfeli and C. Beeson, Infect. Disord. Drug Targets, 2007, 7, 213–220. 8 (a) J. A. Ferreras, J.-S. Ryu, F. Di Lello, D. S. Tan and L. E. N. Quadri, Nat. Chem. Biol., 2005, 1, 29–32; (b) R. V. Somu, H. Boshoff, C. Qiao, E. M. Bennett, C. E. Barry III and C. C. Aldrich, J. Med. Chem., 2006, 49, 31–34. 9 T. V. Inglesby, T. O0Toole, D. A. Henderson, J. G. Bartlett, M. S. Ascher, E. Eitzen, A. M. Friedlander, J. Gerberding, J. Hauer, J. Hughes, J. McDade, M. T. Osterholm, G. Parker, T. M. Perl, P. K. Russell and K. Tonat, J. Am. Med. Assoc., 2002, 287, 2236–2252. 10 S. Cendrowski, W. MacArthur and P. Hanna, Mol. Microbiol., 2004, 51, 407–417. 11 M. K. Wilson, R. J. Abergel, K. N. Raymond, J. E. L. Arceneaux and B. R. Byers, Biochem. Biophys. Res. Commun., 2006, 348, 320–325. 12 R. J. Abergel, M. K. Wilson, J. E. L. Arceneaux, T. M. Hoette, R. K. Strong, B. R. Byers and K. N. Raymond, Proc. Natl. Acad. Sci. U. S. A., 2006, 103, 18499–18503. 13 B. F. Pfleger, J. Y. Lee, R. V. Somu, C. C. Aldrich, P. C. Hanna and D. H. Sherman, Biochemistry, 2007, 46, 4147–4157. 14 M. X. Wu and K. A. W. Hill, Anal. Biochem., 1993, 211, 320–323. |
| URI: | http://wrap.warwick.ac.uk/id/eprint/29337 |
Data sourced from Thomson Reuters' Web of Knowledge
Actions (login required)
 |
View Item |
