Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium

Azim, N. and Deery, Evelyne and Warren, Martin J. and Erskine, Peter T. and Cooper, J. B. and Wood, S.P. and Akhtar, M. (2013) Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 69 (8). pp. 906-908. ISSN 1744-3091. (doi:https://doi.org/10.1107/S1744309113018526) (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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Official URL
http://dx.doi.org/10.1107/S1744309113018526

Abstract

The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 2.5.1.61) catalyses an early step of the tetrapyrrole-biosynthesis pathway in which four molecules of the monopyrrole porphobilinogen are condensed to form a linear tetrapyrrole. The enzyme possesses a dipyrromethane cofactor which is covalently linked by a thioether bridge to an invariant cysteine residue. Expression in Escherichia coli of a His-tagged form of Bacillus megaterium PBGD permitted the crystallization and preliminary X-ray analysis of the enzyme from this species at high resolution.

Item Type: Article
Uncontrolled keywords: tetrapyrrole biosynthesis; porphobilinogen deaminase; Bacillus megaterium; dipyrromethane cofactor
Subjects: Q Science
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: Sue Davies
Date Deposited: 15 Nov 2013 12:00 UTC
Last Modified: 04 Jul 2014 10:46 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/36462 (The current URI for this page, for reference purposes)
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