Sandbox Reserved 320: Difference between revisions
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==Structure== | ==Structure== | ||
E-PPase, a homohexameric protein <ref name = "wong"> PMID: 5498422 </ref>, contains 175 amino-acid residues in each subunit <ref name = "lahti"> PMID: 2848015 </ref>. The protein's topology is described as a five stranded β-barrel that is distorted, highly twisted, and composted of strands β1, β4, β5, β6 and β7, capped on top with α-helix B and the bottom by a loop between strand five and strand six <ref name = "kankare"/>. The active site exists in the bowl formed by the <scene name='Sandbox_Reserved_320/Excursions/1'>excursions</scene> <ref name = "kankare"/>. | E-PPase, a homohexameric protein <ref name = "wong"> PMID: 5498422 </ref>, contains 175 amino-acid residues in each subunit <ref name = "lahti"> PMID: 2848015 </ref>. The protein's topology is described as a five stranded β-barrel that is distorted, highly twisted, and composted of strands β1, β4, β5, β6 and β7, capped on top with α-helix B and the bottom by a loop between strand five and strand six <ref name = "kankare"/>. The active site exists in the bowl formed by the <scene name='Sandbox_Reserved_320/Excursions/1'>excursions</scene> <ref name = "kankare"/>. | ||
==Function== | ==Function== | ||
PPases act to cleave PPi as it is a byproduct in many biosynthetic reactions that include protein, RNA and DNA synthesis<ref name = "kankare"/>. By cleaving the PPi in these synthesis reactions it shifts the equilibrium constants towards biosynthesis <ref name ="kankare"/>. In order to achieve PPi cleavage PPases require a divalent metal ion, usually magnesium <ref name = "kankare"/>. Calcium, alternatively, has been shown to fully suppress PPase activity <ref name = "samygina"/>. PPi hydrolysis is a complicated process that is still not fully understood <ref name = "samygina"/>. | |||
=References= | =References= | ||
<references/> | <references/> | ||
