Issue 20, 2003
From the journal:

Organic & Biomolecular Chemistry

The mechanism of 7,8-diaminopelargonate synthase; the role of S-adenosylmethionine as the amino donor

Rachel S. Breen,a   Dominic J. Campopiano,a   Scott Webster,a   Mhairi Brunton,a   Rory Watta  and  Robert L. Baxter*a  

* Corresponding authors

a Department of Chemistry, Joseph Black Building, The University of Edinburgh, West Mains Road, Edinburgh, UK
E-mail: r.baxter@ed.ac.uk
Tel: +44(0)131 6504708

Abstract

The product of the first transamination step in the reaction catalysed by diaminopelargonate (DAPA) synthase has been shown to be 4-(S-adenosyl)-2-oxobutanoate, which has been trapped as the corresponding alcohol.

Graphical abstract: The mechanism of 7,8-diaminopelargonate synthase; the role of S-adenosylmethionine as the amino donor

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Article information

DOI
https://doi.org/10.1039/B310443P
Article type
Communication
Submitted
28 Aug 2003
Accepted
01 Sep 2003
First published
11 Sep 2003

Org. Biomol. Chem., 2003,1, 3498-3499

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The mechanism of 7,8-diaminopelargonate synthase; the role of S-adenosylmethionine as the amino donor

R. S. Breen, D. J. Campopiano, S. Webster, M. Brunton, R. Watt and R. L. Baxter, Org. Biomol. Chem., 2003, 1, 3498 DOI: 10.1039/B310443P

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