farnesyl diphosphate + protein-cysteine $rightleftharpoons$ S-farnesyl protein + diphosphate

Thus, the two substrates of this enzyme are farnesyl diphosphate and protein-cysteine, whereas its two products are S-farnesyl protein and diphosphate.

This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is farnesyl-diphosphate:protein-cysteine farnesyltransferase. This enzyme is also called FTase.

Structural studies

As of late 2007, 15 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , , , , , and .

References

• Furfine ES, Leban JJ, Landavazo A, Moomaw JF, Casey PJ "Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release". Biochemistry. 34 6857–62.
• Casey PJ, Seabra MC "Protein prenyltransferases". J. Biol. Chem. 271 5289–92.
• Long SB, Casey PJ, Beese LS "Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate". Biochemistry. 37 9612–8.
• 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 12254–65.
• Long SB, Casey PJ, Beese LS "Reaction path of protein farnesyltransferase at atomic resolution". Nature. 419 645–50.
• Sinnott, M. (Ed.), Comprehensive Biological Catalysis. A Mechanistic Reference, vol. 1, Academic Press, San Diego, CA, 1998, p. 31-118.

External links

Gene Ontology (GO) codes