Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution

Azim, N.; Deery, E.; Warren, M.J.; Wolfenden, B.A.A.; Erskine, P.; Cooper, J.B.; Coker, A.; Wood, S.P.; Akhtar, M.

doi:10.1107/S139900471303294X

Acta Crystallographica Section D

Acta Crystallographica

Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 2

The dipyrromethane cofactor of porphobilinogen deaminase is covalently attached to the enzyme by a thioether bond to a cysteine residue. Four substrate pyrroles are added linearly to the cofactor; finally, hydrolysis of the linkage between the substrate and the cofactor releases the tetrapyrrole product hydroxymethylbilane.

BIOLOGICAL

CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 3| February 2014| Pages 744-751

doi:10.1107/S139900471303294X

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