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{{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"/>. | + | 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"/>. |
== '''Inorganic Pyrophosphatase''' == | == '''Inorganic Pyrophosphatase''' == | ||
| - | + | 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>. | |
__TOC__ | __TOC__ | ||
Revision as of 22:36, 31 March 2011
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| 1faj, resolution 2.15Å () | |||||||||
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| Activity: | Inorganic diphosphatase, with EC number 3.6.1.1 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Soluble inorganic pyrophosphatase is a ubiquitous enzyme that plays an important role in energy metabolism [1]. Energy metabolism is made possible by soluble inorganic pyrophosphatases (PPases) by their hydrolyzing inorganic phosphates into two molecules of orthophosphate [2]. PPases may have had an important role in evolution by aiding in accurate DNA copying during chromosome duplication [1]. Escherichia coli (E-coli bacteria) and Saccharomyces cerevisiae (S. cerevisiae yeast) PPases, E-PPase and Y-PPase respectively, are the two best studied PPases [1].
Inorganic Pyrophosphatase
E-PPase, a homohexameric protein [3], contains 175 amino-acid residues in each subunit [4].
Contents |
Structure
Function
References
- ↑ 1.0 1.1 1.2 Kankare J, Neal GS, Salminen T, Glumoff T, Glumhoff T [corrected to Glumoff T, Cooperman BS, Lahti R, Goldman A. The structure of E.coli soluble inorganic pyrophosphatase at 2.7 A resolution. Protein Eng. 1994 Jul;7(7):823-30. PMID:7971944
- ↑ Samygina VR, Popov AN, Rodina EV, Vorobyeva NN, Lamzin VS, Polyakov KM, Kurilova SA, Nazarova TI, Avaeva SM. The structures of Escherichia coli inorganic pyrophosphatase complexed with Ca(2+) or CaPP(i) at atomic resolution and their mechanistic implications. J Mol Biol. 2001 Nov 30;314(3):633-45. PMID:11846572 doi:10.1006/jmbi.2001.5149
- ↑ Wong SC, Burton PM, Josse J. Constitutive inorganic pyrophosphatase of Escherichia coli. V. Reconstitution of native enzyme particles from subunit polypeptide chains. J Biol Chem. 1970 Sep 10;245(17):4353-7. PMID:5498422
- ↑ Lahti R, Pitkaranta T, Valve E, Ilta I, Kukko-Kalske E, Heinonen J. Cloning and characterization of the gene encoding inorganic pyrophosphatase of Escherichia coli K-12. J Bacteriol. 1988 Dec;170(12):5901-7. PMID:2848015
