Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis

Mills-Davies, N.; Butler, D.; Norton, E.; Thompson, D.; Sarwar, M.; Guo, J.; Gill, R.; Azim, N.; Coker, A.; Wood, S.P.; Erskine, P.T.; Coates, L.; Cooper, J.B.; Rashid, N.; Akhtar, M.; Shoolingin-Jordan, P.M.

doi:10.1107/S2059798316019525

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 1
The reaction catalysed by 5-aminolaevulinic acid dehydratase or porphobilinogen synthase (PBGS). The two 5-aminolaevulinic acid moieties forming the acetate (A) and propionate (P) side groups of the product, porphobilinogen, are shown. The next enzyme in the pathway, porphobilinogen deaminase (PBGD), catalyses the condensation of four porphobilinogen moieties to form the first linear tetrapyrrole of the pathway. The following steps in the pathway lead ultimately to the formation of several key cyclic tetrapyrrole cofactors, including haem and chlorophyll.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 73| Part 1| January 2017| Pages 9-21

https://doi.org/10.1107/S2059798316019525

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