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

Institute of Life Sciences and Healthcare

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

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
Journal	Acta Crystallographica - Section F
Volume	69
Issue number	8
DOIs	https://doi.org/10.1107/S1744309113018526
Publication status	Published - 1 Aug 2013

Keywords

tetrapyrrole biosysthesis
porphobilinogen deaminase
Bacillus megaterium
dipyrromethane cofactor

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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.",

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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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journal = "Acta Crystallographica - Section F",

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TY - JOUR

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.

AU - Erskine, P.

AU - Cooper, J. B.

AU - Wood, S. P.

AU - Akhtar, M.

PY - 2013/8/1

Y1 - 2013/8/1

N2 - 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.

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.

KW - tetrapyrrole biosysthesis

KW - porphobilinogen deaminase

KW - Bacillus megaterium

KW - dipyrromethane cofactor

U2 - 10.1107/S1744309113018526

DO - 10.1107/S1744309113018526

M3 - Article

SN - 1744-3091

VL - 69

SP - 906

EP - 908

JO - Acta Crystallographica - Section F

JF - Acta Crystallographica - Section F

IS - 8

ER -

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

Abstract

Keywords

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