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

Azim, N., Deery, Evelyne, Warren, Martin J., Erskine, Peter T., Cooper, J. B., Wood, S.P., 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: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) (KAR id:36462)

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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
DOI/Identification number:	10.1107/S1744309113018526
Uncontrolled keywords:	tetrapyrrole biosynthesis; porphobilinogen deaminase; Bacillus megaterium; dipyrromethane cofactor
Subjects:	Q Science
Divisions:	Divisions > Division of Natural Sciences > Biosciences
Depositing User:	Susan Davies
Date Deposited:	15 Nov 2013 12:00 UTC
Last Modified:	25 Jun 2020 03:05 UTC
Resource URI:	https://kar.kent.ac.uk/id/eprint/36462 (The current URI for this page, for reference purposes)

University of Kent Author Information

Deery, Evelyne.

Creator's ORCID:	https://orcid.org/0000-0002-8189-678X
CReDIT Contributor Roles:

Warren, Martin J..

Creator's ORCID:	https://orcid.org/0000-0002-6028-6456
CReDIT Contributor Roles:

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