Sandbox Reserved 320: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
{{STRUCTURE_1faj| PDB=1faj | SCENE=}} | {{STRUCTURE_1faj| PDB=1faj | SCENE=}} | ||
Soluble inorganic pyrophosphatase is a ubiquitous enzyme that plays an important role in energy metabolism <ref name= "kankare"> PMID: 7971944</ref>. Energy metabolism is made possible by soluble inorganic pyrophosphatases (PPases) by their hydrolyzing inorganic phosphates into two molecules of orthophosphate <ref name = "samygina"> PMID: 11846572</ref>. PPases may have had an important role in evolution by aiding in accurate DNA copying during chromosome duplication <ref name = "kankare"/>. Escherichia coli (E-coli bacteria) and Saccharomyces cerevisiae (S. cerevisiae yeast) PPases, E-PPase and Y-PPase respectively, are the two best studied PPases <ref name = "kankare"/>. | <scene name='Sandbox_Reserved_320/Ppase/1'>Soluble inorganic pyrophosphatase</scene> is a ubiquitous enzyme that plays an important role in energy metabolism <ref name= "kankare"> PMID: 7971944</ref>. Energy metabolism is made possible by soluble inorganic pyrophosphatases (PPases) by their hydrolyzing inorganic phosphates into two molecules of orthophosphate <ref name = "samygina"> PMID: 11846572</ref>. PPases may have had an important role in evolution by aiding in accurate DNA copying during chromosome duplication <ref name = "kankare"/>. Escherichia coli (E-coli bacteria) and Saccharomyces cerevisiae (S. cerevisiae yeast) PPases, E-PPase and Y-PPase respectively, are the two best studied PPases <ref name = "kankare"/>. | ||
== '''Inorganic Pyrophosphatase''' == | == '''Inorganic Pyrophosphatase''' == | ||
| Line 10: | Line 10: | ||
==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"/>. | [[Image:Figure_1.png|left|thumb|'''Figure 1.''' Reaction catalyzed by Inorganic Pyrophosphatase (PPase)]]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= | <br> | ||
==References== | |||
<references/> | <references/> | ||
