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

Azim, N., Deery, E., Warren, M. J. ORCID: https://orcid.org/0000-0002-6028-6456, Erskine, P., Cooper, J. B., 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

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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:	bacillus megaterium,dipyrromethane cofactor,porphobilinogen deaminase,tetrapyrrole biosynthesis,biophysics,structural biology,biochemistry,genetics,condensed matter physics ,/dk/atira/pure/subjectarea/asjc/1300/1304
Faculty \ School:	Faculty of Science
Related URLs:	http://www.scopus.com/inward/record.url?...
Depositing User:	LivePure Connector
Date Deposited:	20 Sep 2022 14:31
Last Modified:	25 Oct 2022 13:31
URI:	https://ueaeprints.uea.ac.uk/id/eprint/88502
DOI:	10.1107/S1744309113018526

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