The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 2.5.1.58     
Accepted name: protein farnesyltransferase
Reaction: farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate
Other name(s): FTase
Systematic name: farnesyl-diphosphate:protein-cysteine farnesyltransferase
Comments: This enzyme, along with protein geranylgeranyltransferase types I (EC 2.5.1.59) and II (EC 2.5.1.60), constitutes the protein prenyltransferase family of enzymes. Catalyses the formation of a thioether linkage between the C-1 of an isoprenyl group and a cysteine residue fourth from the C-terminus of the protein. These protein acceptors have the C-terminal sequence CA1A2X, where the terminal residue, X, is preferably serine, methionine, alanine or glutamine; leucine makes the protein a substrate for EC 2.5.1.59. The enzymes are relaxed in specificity for A1, but cannot act if A2 is aromatic. Substrates of the prenyltransferases include Ras, Rho, Rab, other Ras-related small GTP-binding proteins, γ-subunits of heterotrimeric G-proteins, nuclear lamins, centromeric proteins and many proteins involved in visual signal transduction. A zinc metalloenzyme that requires Mg2+ for activity.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 131384-38-8
References:
1.  Furfine, E.S., Leban, J.J., Landavazo, A., Moomaw, J.F. and Casey, P.J. Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. Biochemistry 34 (1995) 6857–6862. [PMID: 7756316]
2.  Casey, P.J. and Seabra, M.C. Protein prenyltransferases. J. Biol. Chem. 271 (1996) 5289–5292. [PMID: 8621375]
3.  Long, S.B., Casey, P.J. and Beese, L.S. Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. Biochemistry 37 (1998) 9612–9618. [PMID: 9657673]
4.  Micali, E., Chehade, K.A., Isaacs, R.J., Andres, D.A. and Spielmann, H.P. Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. Biochemistry 40 (2001) 12254–12265. [PMID: 11591144]
5.  Long, S.B., Casey, P.J. and Beese, L.S. Reaction path of protein farnesyltransferase at atomic resolution. Nature 419 (2002) 645–650. [PMID: 12374986]
6.  Gibbs, R.A. Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis. In: Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998, pp. 31–118.
[EC 2.5.1.58 created 2003]
 
 


Data © 2001–2017 IUBMB
Web site © 2005–2017 Andrew McDonald