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Porphobilinogen Deaminase

PDB ID 3eq1

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3eq1, resolution 2.80Å ()
Ligands: ,
Activity: Hydroxymethylbilane synthase, with EC number 2.5.1.61
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml


Porphobilinogen deaminase (PBGD) also known as Hydroxymethylbilane synthase, is the third enzyme in the heme biosynthesis pathways in mammals[1]. It catalyses the polymerization of four porphobilinogen molecules to yield hydroxymethylbilane, a pyrrole[2]. Porphobilinogen deaminases are able to form surprisingly stable enzyme-substrate complexes with up to four pyrrole substrates interacting with the active site, a feature unique to the group of enzymes[3]. Dipyrromethane, a cofactor unique to porphobilinogen deaminases, is thought to stabilize these interactions[2].

Function

Structure

References

  1. ↑ Gill R, Kolstoe SE, Mohammed F, Al D-Bass A, Mosely JE, Sarwar M, Cooper JB, Wood SP, Shoolingin-Jordan PM. Structure of human porphobilinogen deaminase at 2.8 A: the molecular basis of acute intermittent porphyria. Biochem J. 2009 Apr 28;420(1):17-25. PMID:19207107 doi:10.1042/BJ20082077
  2. ↑ 2.0 2.1 Jordan PM, Warren MJ. Evidence for a dipyrromethane cofactor at the catalytic site of E. coli porphobilinogen deaminase. FEBS Lett. 1987 Dec 10;225(1-2):87-92. PMID:3079571
  3. ↑ Anderson PM, Desnick RJ. Purification and properties of uroporphyrinogen I synthase from human erythrocytes. Identification of stable enzyme-substrate intermediates. J Biol Chem. 1980 Mar 10;255(5):1993-9. PMID:7354069
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