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Bisucaberin biosynthesis : an adenylating domain of the BibC multi-enzyme catalyzes cyclodimerization of N-hydroxy-N-succinylcadaverine
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Kadi, Nadia, Song, Lijiang and Challis, Gregory L. (2008) Bisucaberin biosynthesis : an adenylating domain of the BibC multi-enzyme catalyzes cyclodimerization of N-hydroxy-N-succinylcadaverine. Chemical Communications (No.41). pp. 5119-5121. doi:10.1039/b813029a
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Official URL: http://dx.doi.org/10.1039/b813029a
Abstract
The bisucaberin biosynthetic gene cluster has been identified in Vibrio salmonicida and a domain from within the BibC multienzyme encoded by the cluster has been shown to catalyse ATP-dependent dimerisation and macrocyclisation of N-hydroxy-N-succinylcadaverine to form bisucaberin.
| Item Type: | Journal Article | ||||
|---|---|---|---|---|---|
| Subjects: | Q Science > QD Chemistry | ||||
| Divisions: | Faculty of Science > Chemistry | ||||
| Library of Congress Subject Headings (LCSH): | Macrocyclic compounds, Multienzyme complexes, Biosynthesis, Deferoxamine -- Synthesis, Genes, Catalysis | ||||
| Journal or Publication Title: | Chemical Communications | ||||
| Publisher: | Royal Society of Chemistry | ||||
| ISSN: | 1359-7345 | ||||
| Official Date: | 7 November 2008 | ||||
| Dates: |
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| Number: | No.41 | ||||
| Number of Pages: | 3 | ||||
| Page Range: | pp. 5119-5121 | ||||
| DOI: | 10.1039/b813029a | ||||
| 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/S/B14450 (BBSRC) |
Data sourced from Thomson Reuters' Web of Knowledge
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