Pyrophosphatase
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| Pyrophosphatase | |||||||||
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| Identifiers | |||||||||
| EC no. | 3.6.1.- | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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Pyrophosphatases, also known as diphosphatases, are acid anhydride hydrolases that act upon diphosphate bonds.[1]
Examples include:
- Inorganic pyrophosphatase, which acts upon the free pyrophosphate ion
- Tobacco acid pyrophosphatase, which catalyses the hydrolysis of a phosphoric ester
- Various organic pyrophosphatases, which act upon organic molecules with the pyrophosphate group (but excluding triphosphatases that act on the final bond):
- Thiamine pyrophosphatase
See also
- List of EC numbers (EC 3) § 3.6.1: In phosphorus-containing anhydrides
References
- ^ Kukko-Kalske E, Heinonen J (1985). "Inorganic pyrophosphate and inorganic pyrophosphatase in Escherichia coli". The International Journal of Biochemistry. 17 (5): 575–80. doi:10.1016/0020-711x(85)90288-5. PMID 2993053.
External links
- Pyrophosphatases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
- v
- t
- e
Hydrolases: acid anhydride hydrolases (EC 3.6)
- Pyrophosphatase
- Apyrase
- Thiamine-triphosphatase
| 3.6.3 |
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| 3.6.4 |
| 3.6.5.1: Heterotrimeric G protein | |
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| 3.6.5.2: Small GTPase > Ras superfamily | |
| 3.6.5.3: Protein-synthesizing GTPase | |
| 3.6.5.5-6: Polymerization motors |
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