ExplorEnz: EC 2.5.1.58

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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, Gene, 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. [DOI] [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. [DOI] [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. [DOI] [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. [DOI] [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]