Farnesyltranstransferase
| farnesyltranstransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.29 | ||||||||
| CAS no. | 9032-58-0 | ||||||||
| 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 farnesyltranstransferase (EC 2.5.1.29) is an enzyme that catalyzes the chemical reaction.
- trans,trans-farnesyl diphosphate + isopentenyl diphosphate diphosphate + geranylgeranyl diphosphate
Thus, the two substrates of this enzyme are trans,trans-farnesyl diphosphate and isopentenyl diphosphate, whereas its two products are diphosphate and geranylgeranyl diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is trans,trans-farnesyl-diphosphate:isopentenyl-diphosphate farnesyltranstransferase. Other names in common use include geranylgeranyl-diphosphate synthase, geranylgeranyl pyrophosphate synthetase, geranylgeranyl-PP synthetase, farnesyltransferase, and geranylgeranyl pyrophosphate synthase. This enzyme participates in biosynthesis of steroids and terpenoid biosynthesis.
This protein may use the morpheein model of allosteric regulation.[1]
Structural studies
[edit]As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2DH4 and 2Q80.
References
[edit]- ^ T. Selwood; E. K. Jaffe. (2011). "Dynamic dissociating homo-oligomers and the control of protein function". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.
- Sagami H, Ishi K, Ogura K (1981). "Occurrence and unusual properties of geranylgeranyl pyrophosphate synthetase of pig liver". Biochem. Int. 3: 669–675.
