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. | |
| 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 |
| Institutional Unit: | Schools > School of Natural Sciences > Biosciences |
| Former Institutional Unit: |
Divisions > Division of Natural Sciences > Biosciences
|
| Depositing User: | Susan Davies |
| Date Deposited: | 15 Nov 2013 12:00 UTC |
| Last Modified: | 20 May 2025 09:18 UTC |
| Resource URI: | https://kar.kent.ac.uk/id/eprint/36462 (The current URI for this page, for reference purposes) |
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