Ontology highlight
ABSTRACT:
SUBMITTER: Azim N
PROVIDER: S-EPMC3729171 | biostudies-literature | 2013 Aug
REPOSITORIES: biostudies-literature
Azim N N Deery E E Warren M J MJ Erskine P P Cooper J B JB Wood S P SP Akhtar M M
Acta crystallographica. Section F, Structural biology and crystallization communications 20130727 Pt 8
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 ...[more]