Porphobilinogen synthase

From Proteopedia

Yeast porphobilinogen synthase complex with laevulunic acid and Zn+2 ion (grey) (PDB entry 1h7n) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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 . The [3]. Water molecules are shown as red spheres.

3D structures of porphobilinogen synthase

Updated on 06-October-2020

References

1. ↑ Jaffe EK. The porphobilinogen synthase catalyzed reaction mechanism. Bioorg Chem. 2004 Oct;32(5):316-25. PMID:15381398 doi:http://dx.doi.org/10.1016/j.bioorg.2004.05.010
2. ↑ 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
3. ↑ 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