Farnesyl-diphosphate kinase
| farnesyl diphosphate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.4.18 | ||||||||
| CAS no. | 50936-43-1 | ||||||||
| 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 farnesyl-diphosphate kinase (EC 2.7.4.18) is an enzyme that catalyzes the chemical reaction
- ATP + farnesyl diphosphate ADP + farnesyl triphosphate
Thus, the two substrates of this enzyme are ATP and farnesyl diphosphate, whereas its two products are ADP and .
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:farnesyl-diphosphate phosphotransferase. This enzyme is also called farnesyl pyrophosphate kinase.
References[]
- Shechter I (September 1974). "Phosphate transfer from trans-farnesyl triphosphate to AMP in Gibberella fujikuroi". Biochimica et Biophysica Acta (BBA) - General Subjects. 362 (2): 233–44. doi:10.1016/0304-4165(74)90216-5. PMID 4423368.
Categories:
- EC 2.7.4
- Enzymes of unknown structure
- EC 2.7 stubs