Crystallization and preliminary X-ray characterization of the tetrapyrrole-biosynthetic enzyme porphobilinogen deaminase from Bacillus megaterium

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

doi:10.1107/S1744309113018526

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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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 and, finally, hydrolysis of the linkage between the substrate and the cofactor releases the tetrapyrrole product hydroxymethylbilane.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 69| Part 8| July 2013| Pages 906-908

doi:10.1107/S1744309113018526

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