Sandbox Reserved 349: Difference between revisions
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='''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>. | 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:00145793</ref> | ||
=Function= | =Function= | ||
Revision as of 01:28, 27 February 2011
Porphobilinogen Deaminase
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| 3eq1, resolution 2.80Å (default scene) | |||||||||||||
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| Ligands: | DPM, SO4 | ||||||||||||
| Activity: | Hydroxymethylbilane synthase, with EC number 2.5.1.61 | ||||||||||||
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| 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[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
- ↑ Lopes MG, Pereirinha A, De Padua F. Intraventricular conduction defects associated with hypertrophic myocardiopathy-an echocardiographic and vectorcardiographic study. Adv Cardiol. 1978;21:223-7. doi: 10.1159/000400454. PMID:145793 doi:https://dx.doi.org/10.1159/000400454
