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Article

Structure of porphobilinogen synthase from Pseudomonas aeruginosa in complex with 5-fluorolevulinic acid suggests a double Schiff base mechanism.

Journal of molecular biology - 5 Jul 2002

Frère Frederic, Schubert Wolf-Dieter, Stauffer Frédéric, Frankenberg Nicole, Neier Reinhard, Jahn Dieter, Heinz Dirk W

Abstract excerpt

All natural tetrapyrroles, including hemes, chlorophylls and vitamin B12, share porphobilinogen (PBG) as a common precursor. Porphobilinogen synthase (PBGS) synthesizes PBG through the asymmetric condensation of two molecules of aminolevulinic acid (ALA). Crystal structures of PBGS from various sources confirm the presence of two distinct binding sites for each ALA molecule, termed A and P. We have solved the...

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PMID: 12079382
DOI: 10.1016/S0022-2836(02)00472-2

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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