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

N. Azim; E. Deery; M. J. Warren; P. Erskine; J. B. Cooper; S. P. Wood; M. Akhtar

doi:10.1107/S1744309113018526

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

N. Azim, E. Deery, M. J. Warren, P. Erskine, J. B. Cooper, S. P. Wood, M. Akhtar

Faculty of Science

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

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.

Original language	English
Pages (from-to)	906-908
Number of pages	3
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	69
Issue number	8
DOIs	https://doi.org/10.1107/S1744309113018526
Publication status	Published - Aug 2013

Keywords

Bacillus megaterium
dipyrromethane cofactor
porphobilinogen deaminase
tetrapyrrole biosynthesis

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10.1107/S1744309113018526Licence: CC BY

Cite this

Azim, N., Deery, E., Warren, M. J., Erskine, P., 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), 906-908. https://doi.org/10.1107/S1744309113018526

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

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.",

keywords = "Bacillus megaterium, dipyrromethane cofactor, porphobilinogen deaminase, tetrapyrrole biosynthesis",

author = "N. Azim and E. Deery and Warren, {M. J.} and P. Erskine and Cooper, {J. B.} and Wood, {S. P.} and M. Akhtar",

year = "2013",

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doi = "10.1107/S1744309113018526",

language = "English",

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Azim, N, Deery, E, Warren, MJ, Erskine, P, Cooper, JB, Wood, SP & 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, vol. 69, no. 8, pp. 906-908. https://doi.org/10.1107/S1744309113018526

Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium. / Azim, N.; Deery, E.; Warren, M. J. et al.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 69, No. 8, 08.2013, p. 906-908.

Research output: Contribution to journal › Article › peer-review

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T1 - Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium

AU - Azim, N.

AU - Deery, E.

AU - Warren, M. J.

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AU - Akhtar, M.

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AB - 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.

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

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Keywords

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