Crystallization and preliminary X‐ray characterization of the tetrapyrrole‐biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium. Issue 8 (31st July 2013)

• Record Type: Journal Article
• Authors: Azim, N.; Deery, E.; Warren, M. J.; Erskine, P.; Cooper, J. B.; Wood, S. P.; Akhtar, M.
• Is Part Of: Acta crystallographica. Volume 69:Issue 8(2013:Aug.)
• Page Start: 906
• Page End: 908
• Publication Date: 2013-07-31
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113018526
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>Escherichia coli</italic> of a His‐tagged form of <italic>Bacillus megaterium</italic> PBGD permitted the crystallization and preliminary X‐ray analysis of the enzyme from this species at high resolution.</p> </abstract>