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 1
The reaction catalysed by porphobilinogen deaminase. Four molecules of the pyrrole porphobilinogen are condensed to form the linear tetrapyrrole preuroporphyrinogen (hydroxymethylbilane). The acetic and propionic acid side chains of each pyrrole are abbreviated A and P, respectively, and the four rings of the tetrapyrrole product are indicated in italics as A, B, C and D.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

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

doi:10.1107/S1744309113018526

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