protein farnesyltransferase;
FTase

Transferases;
Transferring alkyl or aryl groups, other than methyl groups;
Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

farnesyl-diphosphate:protein-cysteine farnesyltransferase

farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate [RN:R09844]

R09844

farnesyl diphosphate [CPD:C00448];
protein-cysteine [CPD:C20119]

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, gamma-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.

1  [PMID:7756316]

Furfine ES, Leban JJ, Landavazo A, Moomaw JF, Casey PJ.

Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release.

Biochemistry. 34 (1995) 6857-62.

Rattus norvegicus [GN:rno], Bos taurus [GN:bta]

2  [PMID:8621375]

Casey PJ, Seabra MC.

Protein prenyltransferases.

J. Biol. Chem. 271 (1996) 5289-92.

Homo sapiens [GN:hsa], Rattus norvegicus [GN:rno], Saccharomyces cerevisiae [GN:sce]

3  [PMID:9657673]

Long SB, Casey PJ, Beese LS.

Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate.

Biochemistry. 37 (1998) 9612-8.

Rattus norvegicus [GN:rno]

4  [PMID:11591144]

Micali E, Chehade KA, Isaacs RJ, Andres DA, Spielmann HP.

Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups.

Biochemistry. 40 (2001) 12254-65.

Rattus norvegicus [GN:rno]

5  [PMID:12374986]

Long SB, Casey PJ, Beese LS.

Reaction path of protein farnesyltransferase at atomic resolution.

Nature. 419 (2002) 645-50.

Homo sapiens [GN:hsa]

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, p. 31-118.