Farnesyltransferase
| Farnesyltransferase | ||
|---|---|---|
|
Vorhandene Strukturdaten: s. UniProt | ||
| Eigenschaften des menschlichen Proteins | ||
| Masse/Länge Primärstruktur | 816 = 379+437 Aminosäuren | |
| Sekundär- bis Quartärstruktur | A+B | |
| Kofaktor | Zn (B) | |
| Bezeichner | ||
| Gen-Namen | FNTA, FTNB | |
| Externe IDs | ||
| Enzymklassifikation | ||
| EC, Kategorie | 2.5.1.58, Transferase | |
| Reaktionsart | Prenylierung | |
| Substrat | Farnesyldiphosphat + Protein | |
| Produkte | S-Farnesyl-Protein + Diphosphat | |
| Vorkommen | ||
| Homologie-Familie | FTase | |
| Übergeordnetes Taxon | Eukaryoten | |
Farnesyltransferase (Abk. FTase) ist dasjenige Enzym, das die Übertragung eines Farnesylrests von Farnesyldiphosphat (FPP) auf Proteine katalysiert. Durch die so entstandene Thioetherbindung zwischen Farnesylrest und C-terminalen Cystein des Proteins kann Letzteres an die Zellmembran verankert werden. Dieser Mechanismus wird auch als (posttranslationale) Prenylierung bezeichnet und kommt in allen Eukaryoten vor.
Die FTase besteht beim Menschen aus zwei Untereinheiten und ist außerdem in der Lage, Geranylgeranylreste zu übertragen (EC 2.5.1.59).
Literatur
- T. S. Reid, K. L. Terry, P. J. Casey, L. S. Beese: Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. In: J. Mol. Biol. 343 (2), Oktober 2004, S. 417–433. doi:10.1016/j.jmb.2004.08.056. PMID 15451670.
- R. T. Eastman, F. S. Buckner, K. Yokoyama, M. H. Gelb, W. C. Van Voorhis: Thematic review series: lipid posttranslational modifications. Fighting parasitic disease by blocking protein farnesylation. In: J. Lipid Res. 47 (2), February 2006, S. 233–240. doi:10.1194/jlr.R500016-JLR200. PMID 16339110.
- K. T. Lane, L. S. Beese: Thematic review series: lipid posttranslational modifications. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type I. In: J. Lipid Res. 47 (4), April 2006, S. 681–699. doi:10.1194/jlr.R600002-JLR200. PMID 16477080.
- S. B. Long, P. J. Casey, L. S. Beese: Reaction path of protein farnesyltransferase at atomic resolution. In: Nature. 419 (6907), October 2002, S. 645–650. doi:10.1038/nature00986. PMID 12374986.
- A. G. Agrawal, R. R. Somani: Farnesyltransferase inhibitor as anticancer agent. In: Mini-Rev Med Chem. 9 (6), June 2009, S. 638–652. doi:10.2174/138955709788452702. PMID 19519490.
- E. S. Furfine, J. J. Leban, A. Landavazo, J. F. Moomaw, P. J. Casey: Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release. In: Biochemistry. 34 (20), 1995, S. 6857–6862. doi:10.1021/bi00020a032. PMID 7756316.
- P. J. Casey, M. C. Seabra: Protein prenyltransferases. In: J. Biol. Chem. 271 (10), 1996, S. 5289–5292. doi:10.1074/jbc.271.10.5289. PMID 8621375.
- S. B. Long, P. J. Casey, L. S. Beese: Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. In: Biochemistry. 37 (27), 1998, S. 9612–9618. doi:10.1021/bi980708e. PMID 9657673.
- E. Micali, K. A. Chehade, R. J. Isaacs, D. A. Andres, H. P. Spielmann: Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups. In: Biochemistry. 40 (41), 2001, S. 12254–12265. doi:10.1021/bi011133f. PMID 11591144.
- M. Sinnott (Hrsg.): Comprehensive Biological Catalysis. A Mechanistic Reference. vol. 1, Academic Press, San Diego, CA 1998, S. 31–118.
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