EC - Protein farnesyltransferase

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IntEnz Enzyme Nomenclature


Accepted name:
protein farnesyltransferase
Other name:
Systematic name:
farnesyl-diphosphate:protein-cysteine farnesyltransferase




This enzyme, along with geranylgeranyltransferase types I (EC and II (EC, 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 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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00703
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004660
UniProtKB/Swiss-Prot: (23) [show] [UniProt]


  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 : 6857-6862 (1995). [PMID: 7756316]
  2. Casey, P.J. and Seabra, M.C.
    Protein prenyltransferases.
    J. Biol. Chem. 271 : 5289-5292 (1996). [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 : 9612-9618 (1998). [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 : 12254-12265 (2001). [PMID: 11591144]
  5. Long, S.B., Casey, P.J. and Beese, L.S.
    Reaction path of protein farnesyltransferase at atomic resolution.
    Nature 419 : 645-650 (2002). [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 , 1998 , 31-118

[EC created 2003]