guanosine-triphosphate guanylyltransferase | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC no. | 2.7.7.45 | ||||||||
CAS no. | 54576-89-5 | ||||||||
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 guanosine-triphosphate guanylyltransferase (EC 2.7.7.45) is an enzyme that catalyzes the chemical reaction
- 2 GTP diphosphate + P1,P4-bis(5'-guanosyl) tetraphosphate
Hence, this enzyme has one substrate, GTP, and two products, diphosphate and P1,P4-bis(5'-guanosyl) tetraphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:GTP guanylyltransferase. Other names in common use include diguanosine tetraphosphate synthetase, GTP-GTP guanylyltransferase, Gp4G synthetase, and guanosine triphosphate-guanose triphosphate guanylyltransferase.
References
- Warner AH, Beers PC, Huang FL (1974). "Biosynthesis of the diguanosine nucleotides. I. Purification and properties of an enzyme from yolk platelets of brine shrimp embryos". Can. J. Biochem. 52 (3): 231–40. doi:10.1139/o74-036. PMID 4208243.
Transferases: phosphorus-containing groups (EC 2.7) | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
2.7.1-2.7.4: phosphotransferase/kinase (PO4) |
| ||||||||||||||
2.7.6: diphosphotransferase (P2O7) | |||||||||||||||
2.7.7: nucleotidyltransferase (PO4-nucleoside) |
| ||||||||||||||
2.7.8: miscellaneous |
| ||||||||||||||
2.7.10-2.7.13: protein kinase (PO4; protein acceptor) |
|
Enzymes | |
---|---|
Activity | |
Regulation | |
Classification | |
Kinetics | |
Types |
|
This EC 2.7 enzyme-related article is a stub. You can help Misplaced Pages by expanding it. |