The enzyme porphobilinogen deaminase (PBGD; hydroxymethylbilane synthase; EC 126.96.36.199) 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.
|Number of pages||3|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Publication status||Published - Aug 2013|
- Bacillus megaterium
- dipyrromethane cofactor
- porphobilinogen deaminase
- tetrapyrrole biosynthesis