GTP diphosphokinase
| GTP diphosphokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.6.5 | ||||||||
| CAS no. | 63690-89-1 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a GTP diphosphokinase (EC 2.7.6.5) is an enzyme that catalyzes the chemical reaction
- ATP + GTP AMP + guanosine 3'-diphosphate 5'-triphosphate
Thus, the two substrates of this enzyme are ATP and GTP, whereas its two products are AMP and guanosine 3'-diphosphate 5'-triphosphate.
This enzyme belongs to the family of transferases, specifically those transferring two phosphorus-containing groups (diphosphotransferases). The systematic name of this enzyme class is ATP:GTP 3'-diphosphotransferase. Other names in common use include stringent factor, guanosine 3',5'-polyphosphate synthase, GTP pyrophosphokinase, ATP-GTP 3'-diphosphotransferase, guanosine 5',3'-polyphosphate synthetase, (p)ppGpp synthetase I, (p)ppGpp synthetase II, guanosine pentaphosphate synthetase, GPSI, and GPSII. This enzyme participates in purine metabolism.
Structural studies
[edit | edit source]As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1E3H, 1E3P, 1VJ7, and 2BE3.
References
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