Protein farneziltransferaza
| Protein farneziltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.5.1.58 | ||||||||
| CAS broj | 131384-38-8 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Protein farneziltransferaza (EC 2.5.1.58, FTaze) je enzim sa sistematskim imenom farnezil-difosfat:protein-cistein farneziltransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- farnezil difosfat + protein-cistein S-farnezil protein + difosfat
Ovaj enzim, zajedno sa proteinskom geranilgeraniltransferazom tip I (EC 2.5.1.59) i II (EC 2.5.1.60) sačinjava proteinsku preniltransferaznu familiju enzima.
Reference
- ↑ Furfine, E.S., Leban, J.J., Landavazo, A., Moomaw, J.F. and Casey, P.J. (1995). „Protein farnesyltransferase: kinetics of farnesyl pyrophosphate binding and product release”. Biochemistry 34: 6857-6862. PMID 7756316.
- ↑ Casey, P.J. and Seabra, M.C. (1996). „Protein prenyltransferases”. J. Biol. Chem. 271: 5289-5292. PMID 8621375.
- ↑ Long, S.B., Casey, P.J. and Beese, L.S. (1998). „Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate”. Biochemistry 37: 9612-9618. PMID 9657673.
- ↑ Micali, E., Chehade, K.A., Isaacs, R.J., Andres, D.A. and Spielmann, H.P. (2001). „Protein farnesyltransferase isoprenoid substrate discrimination is dependent on isoprene double bonds and branched methyl groups”. Biochemistry 40: 12254-12265. PMID 11591144.
- ↑ Long, S.B., Casey, P.J. and Beese, L.S. (2002). „Reaction path of protein farnesyltransferase at atomic resolution”. Nature 419: 645-650. PMID 12374986.
- ↑ Gibbs, R.A. (1998). „Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis”. u: Sinnott, M.. Comprehensive Biological Catalysis. A Mechanistic Reference. 1. San Diego, CA: Academic Press. str. 31-118.
Literatura
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.
- Gibbs, R.A. (1998). „Prenyl transfer and the enzymes of terpenoid and steroid biosynthesis”. u: Sinnott, M.. Comprehensive Biological Catalysis. A Mechanistic Reference. 1. San Diego, CA: Academic Press. str. 31-118.
Spoljašnje veze
- MeSH Protein+farnesyltransferase
- p
- r
- u
Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
