Issue 41, 2008
From the journal:

Chemical Communications

Bisucaberin biosynthesis: an adenylating domain of the BibC multi-enzyme catalyzes cyclodimerization of N-hydroxy-N-succinylcadaverine†

Nadia Kadi,a   Lijiang Songa  and  Gregory L. Challisa  

a Department of Chemistry, University of Warwick, Coventry, UK
E-mail: g.l.challis@warwick.ac.uk
Fax: 024 7652 4112
Tel: 024 7657 4024

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.

Graphical abstract: Bisucaberin biosynthesis: an adenylating domain of the BibC multi-enzyme catalyzes cyclodimerization of N-hydroxy-N-succinylcadaverine

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Article information

DOI
https://doi.org/10.1039/B813029A
Article type
Communication
Submitted
29 Jul 2008
Accepted
05 Sep 2008
First published
22 Sep 2008

Chem. Commun., 2008, 5119-5121

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Bisucaberin biosynthesis: an adenylating domain of the BibC multi-enzyme catalyzes cyclodimerization of N-hydroxy-N-succinylcadaverine

N. Kadi, L. Song and G. L. Challis, Chem. Commun., 2008, 5119 DOI: 10.1039/B813029A

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