Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Arabidopsis thaliana

Roberts, A, Gill, R, Hussey, R J, Mikolajek, H, Erskine, P T, Cooper, J B, Wood, S P, Chrystal, E J T and Shoolingin-Jordan, P M (2012) Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Arabidopsis thaliana. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68 (12). pp. 1491-1493. ISSN 1744-3091

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Abstract

The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 2.5.1.61) catalyses a key early step of the haem-biosynthesis pathway in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole. The enzyme possesses a dipyrro- methane cofactor which is covalently linked by a thioether bridge to an invariant cysteine residue. Since PBGD catalyses a reaction which is common to the biosynthesis of both haem and chlorophyll, structural studies of a plant PBGD enzyme offer great potential for the discovery of novel herbicides. Until recently, structural data have only been available for the Escherichia coli and human forms of the enzyme. Expression in E. coli of a codon-optimized gene for Arabidopsis thaliana PBGD has permitted for the first time the crystallization and preliminary X-ray analysis of the enzyme from a plant species at high resolution.

Item Type: Article
Schools and Departments: School of Life Sciences > Chemistry
Depositing User: Raj Gill
Date Deposited: 09 Jan 2017 11:45
Last Modified: 09 Jan 2017 11:45
URI: http://sro.sussex.ac.uk/id/eprint/66072
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