Farnesyl transferase

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Farnesyl transferase

Existing structural data: s. UniProt

Properties of human protein
Mass / length primary structure 816 = 379 + 437 amino acids
Secondary to quaternary structure A + B
Cofactor Zn (B)
Identifier
Gene names FNTA  ; FTNB
External IDs
Enzyme classification
EC, category 2.5.1.58 ,  transferase
Response type Prenylation
Substrate Farnesyl diphosphate + protein
Products S-farnesyl protein + diphosphate
Occurrence
Homology family FTase
Parent taxon Eukaryotes

Farnesyl transferase (abbr. FTase ) is the enzyme that catalyzes the transfer of a farnesyl residue from farnesyl diphosphate (FPP) to proteins. The thioether bond created in this way between the farnesyl residue and the C-terminal cysteine ​​of the protein allows the latter to be anchored to the cell membrane . This mechanism is also known as (post-translational) prenylation and occurs in all eukaryotes .

Representation of farnesyl transferase

The FTase consists of two subunits in humans and is also able to transfer geranylgeranyl residues ( EC  2.5.1.59 )

See also

literature

  • TS Reid, KL Terry, PJ Casey, LS Beese: Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. In: J. Mol. Biol. 343 (2), October 2004, pp. 417-433. doi: 10.1016 / j.jmb.2004.08.056 . PMID 15451670 .
  • RT Eastman, FS Buckner, K. Yokoyama, MH Gelb, WC Van Voorhis: Thematic review series: lipid posttranslational modifications. Fighting parasitic disease by blocking protein farnesylation. In: J. Lipid Res. 47 (2), February 2006, pp. 233-240. doi: 10.1194 / jlr.R500016-JLR200 . PMID 16339110 .
  • KT Lane, LS Beese: Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. In: J. Lipid Res. 47 (4), April 2006, pp. 681-699. doi: 10.1194 / jlr.R600002-JLR200 . PMID 16477080 .
  • SB Long, PJ Casey, LS Beese: Reaction path of protein farnesyltransferase at atomic resolution. In: Nature. 419 (6907), October 2002, pp. 645-650. doi: 10.1038 / nature00986 . PMID 12374986 .
  • AG Agrawal, RR Somani: Farnesyltransferase inhibitor as anticancer agent. In: Mini-Rev Med Chem . 9 (6), June 2009, pp. 638-652. doi: 10.2174 / 138955709788452702 . PMID 19519490 .
  • ES Furfine, JJ Leban, A. Landavazo, JF Moomaw, PJ Casey: Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. In: Biochemistry. 34 (20), 1995, pp. 6857-6862. doi: 10.1021 / bi00020a032 . PMID 7756316 .
  • PJ Casey, MC Seabra: Protein prenyltransferases. In: J. Biol. Chem. 271 (10), 1996, pp. 5289-5292. doi: 10.1074 / jbc.271.10.5289 . PMID 8621375 .
  • SB Long, PJ Casey, LS Beese: Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. In: Biochemistry. 37 (27), 1998, pp. 9612-9618. doi: 10.1021 / bi980708e . PMID 9657673 .
  • E. Micali, KA Chehade, RJ Isaacs, DA Andres, HP Spielmann: Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. In: Biochemistry. 40 (41), 2001, pp. 12254-12265. doi: 10.1021 / bi011133f . PMID 11591144 .
  • M. Sinnott (Ed.): Comprehensive Biological Catalysis. A Mechanistic Reference. vol. 1, Academic Press, San Diego, CA 1998, pp. 31-118.