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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. ISSN 1359-7345

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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:

Date	Event
7 November 2008	Published

Number:

No.41

Number of Pages:

Page Range:

pp. 5119-5121

Identification Number:

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)

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