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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

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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:
DateEvent
7 November 2008Published
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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