Function
Porphobilinogen synthase or δ-aminolaevulinic acid dehydratase (PBS) catalyzes the formation of porphobilinogen (PBG) from 2 molecules of aminolaevulinic acid (ALA). PBS participates in porphyrin biosynthesis[1]. Levulinic acid (LA) is an inhibitor of PBS. Porphyrin is the precursor of hemes, chlorophyll and vitamin B12.
Disease
PBS deficiency can be caused by lead and other heavy metal poisoning[2].
Structural highlights
The biological assembly of Yeast porphobilinogen synthase is homooctamer. The active site of PBS contains the substrate laevulinic acid and Zn+2 ion[3]. Water molecules are shown as red spheres.
- ↑ Jaffe EK. The porphobilinogen synthase catalyzed reaction mechanism. Bioorg Chem. 2004 Oct;32(5):316-25. PMID:15381398 doi:https://dx.doi.org/10.1016/j.bioorg.2004.05.010
- ↑ Doss M, Muller WA. Acute lead poisoning in inherited porphobilinogen synthase (delta-aminolevulinic acid dehydrase) deficiency. Blut. 1982 Aug;45(2):131-9. PMID:7104498
- ↑ Erskine PT, Newbold R, Brindley AA, Wood SP, Shoolingin-Jordan PM, Warren MJ, Cooper JB. The x-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with substrate and three inhibitors. J Mol Biol. 2001 Sep 7;312(1):133-41. PMID:11545591 doi:10.1006/jmbi.2001.4947
