X-ray structure of a putative reaction intermediate of 5-aminolaevulinic acid dehydratase

Erskine, Peter T. and Coates, Leighton and Butler, Danica and Youell, James H. and Brindley, Amanda A. and Wood, Steve P. and Warren, Martin J. and Shoolingin-Jordan, Peter M. and Cooper, Jonathan B. (2003) X-ray structure of a putative reaction intermediate of 5-aminolaevulinic acid dehydratase. Biochemical Journal , 373 (Pt 3). pp. 733-8. ISSN 0264-6021 . (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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The X-ray structure of yeast 5-aminolaevulinic acid dehydratase, in which the catalytic site of the enzyme is complexed with a putative cyclic intermediate composed of both substrate moieties, has been solved at 0.16 nm (1.6 A) resolution. The cyclic intermediate is bound covalently to Lys(263) with the amino group of the aminomethyl side chain ligated to the active-site zinc ion in a position normally occupied by a catalytic hydroxide ion. The cyclic intermediate is catalytically competent, as shown by its turnover in the presence of added substrate to form porphobilinogen. The findings, combined with those of previous studies, are consistent with a catalytic mechanism in which the C-C bond linking both substrates in the intermediate is formed before the C-N bond.

Item Type: Article
Uncontrolled keywords: Crystallography, X-Ray Models, Molecular Porphobilinogen Synthase/*chemistry/metabolism Protein Structure, Tertiary Recombinant Proteins/chemistry/metabolism Saccharomyces cerevisiae/enzymology
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Martin Warren
Date Deposited: 09 Oct 2009 08:04
Last Modified: 14 May 2014 15:57
Resource URI: https://kar.kent.ac.uk/id/eprint/11052 (The current URI for this page, for reference purposes)
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