Open AccessCrystallization and preliminary X‐ray characterization of the tetrapyrrole‐biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium
Author(s) -
Azim N.,
Deery E.,
Warren M. J.,
Erskine P.,
Cooper J. B.,
Wood S. P.,
Akhtar M.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113018526
Subject(s) - porphobilinogen deaminase , tetrapyrrole , porphobilinogen , enzyme , chemistry , biochemistry , bacillus megaterium , stereochemistry , porphobilinogen synthase , cofactor , cysteine , heme , biology , dehydratase , bacteria , genetics
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.