EC 2.5.1.58 - Protein farnesyltransferase

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IntEnz Enzyme Nomenclature
EC 2.5.1.58

Names

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

Reaction

Cofactors

Comments:

This enzyme, along with 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

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: (20) [show] [UniProt]

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: 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 2.5.1.58 created 2003]