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)
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. (Contact us about this Publication) | |
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 |
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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) |
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