Guanosine-3',5'-bis(diphosphate) 3'-diphosphatase
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| guanosine-3′,5′-bis(diphosphate) 3′-diphosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.7.2 | ||||||||
| CAS no. | 70457-12-4 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme guanosine-3′,5′-bis(diphosphate) 3′-diphosphatase (EC 3.1.7.2)[1][2] catalyzes the reaction
- guanosine 3′,5′-bis(diphosphate) + H2O GDP + diphosphate
This enzyme belongs to the family of hydrolases, specifically those acting on diphosphoric monoester bonds. The systematic name is guanosine-3′,5′-bis(diphosphate) 3′-diphosphohydrolase. Other names in common use include guanosine-3′,5′-bis(diphosphate) 3′-pyrophosphatase, PpGpp-3'-pyrophosphohydrolase, and PpGpp phosphohydrolase. This enzyme participates in purine metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1VJ7.
References
- ^ Heinemeyer EA, Richter D (1978). "Characterization of the guanosine 5'-triphosphate 3′-diphosphate and guanosine 5′-diphosphate 3′-diphosphate degradation reaction catalyzed by a specific pyrophosphorylase from Escherichia coli". Biochemistry. 17 (25): 5368–72. doi:10.1021/bi00618a007. PMID 365225.
- ^ Richter D, Fehr S, Harder R (1979). "The guanosine 3′,5′-bis(diphosphate) (ppGpp) cycle. Comparison of synthesis and degradation of guanosine 3′,5′-bis(diphosphate) in various bacterial systems". Eur. J. Biochem. 99 (1): 57–64. doi:10.1111/j.1432-1033.1979.tb13230.x. PMID 114395.
