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

journal contribution
posted on 2023-06-09, 04:36 authored by A Roberts, R Gill, R J Hussey, H Mikolajek, P T Erskine, J B Cooper, S P Wood, E J T Chrystal, P M Shoolingin-Jordan
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.

History

Publication status

  • Published

Journal

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

ISSN

1744-3091

Publisher

International Union of Crystallography

Issue

12

Volume

68

Page range

1491-1493

Department affiliated with

  • Chemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2017-01-09

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