Inorganic pyrophosphatase
From Proteopedia
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{{STRUCTURE_2bqy| PDB=2bqy | SIZE=400| SCENE= |right|CAPTION=Inorganic pyrophosphatase complex with pyrophosphate, [[2bqy]] }} | {{STRUCTURE_2bqy| PDB=2bqy | SIZE=400| SCENE= |right|CAPTION=Inorganic pyrophosphatase complex with pyrophosphate, [[2bqy]] }} | ||
| - | + | == Function == | |
'''Inorganic pyrophosphatase''' (PPase) catalyzes the breakdown of pyrophosphate (PPi) to two molecules of phosphate (PO4). The reaction releases energy and is irreversible hence it is coupled to biochemical reactions which need to be driven to completion. PPase plays a role in lipid metabolism, calcium absorption, bone formation and DNA synthesis. PPase requires a divalent metal ion like Mg+2 for higher activity. PPi is formed in many biosynthetic reactions which require ATP<ref>PMID:5342521</ref>. | '''Inorganic pyrophosphatase''' (PPase) catalyzes the breakdown of pyrophosphate (PPi) to two molecules of phosphate (PO4). The reaction releases energy and is irreversible hence it is coupled to biochemical reactions which need to be driven to completion. PPase plays a role in lipid metabolism, calcium absorption, bone formation and DNA synthesis. PPase requires a divalent metal ion like Mg+2 for higher activity. PPi is formed in many biosynthetic reactions which require ATP<ref>PMID:5342521</ref>. | ||
| + | |||
| + | == Structural highlights == | ||
| + | PPase binding pocket has negative electrostatic potential and is composed of 3 lysine residues, a tyrosine and several water molecules<ref>PMID:16988955</ref>. | ||
==3D structures of inorganic pyrophosphatase== | ==3D structures of inorganic pyrophosphatase== | ||
Revision as of 09:56, 28 March 2016
Contents |
Function
Inorganic pyrophosphatase (PPase) catalyzes the breakdown of pyrophosphate (PPi) to two molecules of phosphate (PO4). The reaction releases energy and is irreversible hence it is coupled to biochemical reactions which need to be driven to completion. PPase plays a role in lipid metabolism, calcium absorption, bone formation and DNA synthesis. PPase requires a divalent metal ion like Mg+2 for higher activity. PPi is formed in many biosynthetic reactions which require ATP[1].
Structural highlights
PPase binding pocket has negative electrostatic potential and is composed of 3 lysine residues, a tyrosine and several water molecules[2].
3D structures of inorganic pyrophosphatase
Updated on 28-March-2016
References
- ↑ Harold FM. Inorganic polyphosphates in biology: structure, metabolism, and function. Bacteriol Rev. 1966 Dec;30(4):772-94. PMID:5342521
- ↑ Chao TC, Huang H, Tsai JY, Huang CY, Sun YJ. Kinetic and structural properties of inorganic pyrophosphatase from the pathogenic bacterium Helicobacter pylori. Proteins. 2006 Nov 15;65(3):670-80. PMID:16988955 doi:10.1002/prot.21093
