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Article

Structural studies of domain movement in active-site mutants of porphobilinogen deaminase from Bacillus megaterium.

Acta crystallographica. Section F, Structural biology communications - 1 Nov 2017

Guo Jingxu, Erskine Peter, Coker Alun R, Wood Steve P, Cooper Jonathan B

Abstract excerpt

The enzyme porphobilinogen deaminase (PBGD) is one of the key enzymes in tetrapyrrole biosynthesis. It catalyses the formation of a linear tetrapyrrole from four molecules of the substrate porphobilinogen (PBG). It has a dipyrromethane cofactor (DPM) in the active site which is covalently linked to a conserved cysteine residue through a thioether bridge. The substrate molecules are linked to the cofactor in a...

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PMID: 29095155
DOI: 10.1107/S2053230X17015436
PMCID: PMC5683031

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