Sandbox Reserved 349: Difference between revisions
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Porphobilinogen deaminase (PBGD) also known as Hydroxymethylbilane synthase, is a dimeric polypeptide and 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 precursor in the formation of [[Porphyrin]]<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>. <scene name='Sandbox_Reserved_349/Dpm/1'>Dipyrromethane (DPM)</scene>, a cofactor unique to porphobilinogen deaminases, is thought to stabilize these interactions at each of the two active domains<ref name="Peter">PMID:3079571</ref>. Mutations in the human PBGD gene are responsible for the condition Acute Intermittent Porphyria (AIP) in humans<ref name="Raj">PMID: 19207107</ref>. | Porphobilinogen deaminase (PBGD) also known as Hydroxymethylbilane synthase, is a dimeric polypeptide and 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 precursor in the formation of [[Porphyrin]]<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>. <scene name='Sandbox_Reserved_349/Dpm/1'>Dipyrromethane (DPM)</scene>, a cofactor unique to porphobilinogen deaminases, is thought to stabilize these interactions at each of the two active domains<ref name="Peter">PMID:3079571</ref>. Mutations in the human PBGD gene are responsible for the condition Acute Intermittent Porphyria (AIP) in humans<ref name="Raj">PMID: 19207107</ref>. | ||
=Structure= | =Structure= | ||
<scene name='Template:Sandbox_Reserved_349/Dpm_site/2'>Dipyrromethane</scene> | The human PBGD is three domain polypeptide each consisting of approximately 110 amino acids<ref name="Raj">PMID: 19207107</ref>. in the active site, a unique molecule known as <scene name='Template:Sandbox_Reserved_349/Dpm_site/2'>Dipyrromethane</scene> | ||
<scene name='Template:Sandbox_Reserved_349/Dpm_site/2'>Dipyrromethane</scene> interacts with porphobilinogen and anchors it in place<ref name="Raj">PMID: 19207107</ref>. Ordered sulfate ions are also hydrogen bonded with Arg26 and Ser28 residues that are highly conserved amongst human and ''E.coli'' variants of PBGD<ref name="Raj">PMID: 19207107</ref>. | |||
=Function= | =Function= | ||
