Sandbox Reserved 349
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
='''Porphobilinogen Deaminase'''= | ='''Porphobilinogen Deaminase'''= | ||
{{STRUCTURE_3eq1 | PDB=3eq1 | SCENE= }} | {{STRUCTURE_3eq1 | PDB=3eq1 | SCENE= }} | ||
| - | Porphobilinogen deaminase (PBGD) also known as Hydroxymethylbilane synthase, is the third enzyme in the heme biosynthesis pathways in mammals<ref name="Raj">PMID: 19207107</ref>. It catalyses the polymerization of four porphobilinogen molecules to yield hydroxymethylbilane<ref name="Peter">PMID:3079571</ref> | + | Porphobilinogen deaminase (PBGD) also known as Hydroxymethylbilane synthase, is the third enzyme in the heme biosynthesis pathways in mammals<ref name="Raj">PMID: 19207107</ref>. It catalyses the polymerization of four porphobilinogen molecules to yield hydroxymethylbilane, a pyrrole<ref name="Peter">PMID:3079571</ref>. 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<ref name="Anderson">PMID:7354069</ref>. Dipyrromethane, a cofactor unique to porphobilinogen deaminases, is thought to stabilize these interactions<ref name="Peter">PMID:3079571</ref>. |
=Function= | =Function= | ||
Revision as of 01:47, 27 February 2011
Contents |
Porphobilinogen Deaminase
| |||||||||
| 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
- ↑ 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
- ↑ 2.0 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
- ↑ 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
