Peptidilprolilna izomeraza
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| Peptidilprolilna izomeraza | |||||||||
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| Identifikatori | |||||||||
| EC broj | 5.2.1.8 | ||||||||
| CAS broj | 95076-93-0 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Peptidilprolilna izomeraza (EC 5.2.1.8, PPIaza, ciklofilin, peptid vezana izomeraza, peptidilna-prolil cis-trans izomeraza) je enzim sa sistematskim imenom peptidilprolin cis-trans-izomeraza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju
- peptidilnaprolin (omega = 180) peptidilnaprolin (omega = 0)
Prvi pronađeni tip ovog enzima je proteinski ciklofilin, koji vezuje imunosupresant ciklosporin A. Postoje druge distinktne familije. Među njima su FK-506 vezujući proteini (FKBP).
Reference[uredi | uredi kod]
- ↑ Fischer, G. and Bang, H. (1985). „The refolding of urea-denatured ribonuclease A is catalyzed by peptidyl-prolyl cis-trans isomerase”. Biochim. Biophys. Acta 828: 39-42. PMID 3882150.
- ↑ Fischer, G., Bang, H. and Mech, C. (1984). „[Determination of enzymatic catalysis for the cis-trans-isomerization of peptide binding in proline-containing peptides]”. Biomed. Biochim. Acta 43: 1101-1111. PMID 6395866.
- ↑ Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T. and Schmid, F.X. (1989). „Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins”. Nature 337: 476-478. PMID 2492638.
- ↑ Takahashi, N., Hayano, T. and Suzuki, M. (1989). „Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin”. Nature 337: 473-475. PMID 2644542.
- ↑ Hennig, L., Christner, C., Kipping, M., Schelbert, B., Rucknagel, K.P., Grabley, S., Kullertz, G. and Fischer, G. (1998). „Selective inactivation of parvulin-like peptidyl-prolyl cis/trans isomerases by juglone”. Biochemistry 37: 5953-5960. PMID 9558330.
- ↑ Fischer, G. (1994). „Peptidyl-prolyl cis/trans isomerases and their effectors”. Angew. Chem. Int. Ed. Engl. 33: 1415-1436.
- ↑ Harrison, R.K. and Stein, R.L. (1990). „Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes”. Biochemistry 29: 3813-3816. PMID 1693856.
- ↑ Eisenmesser, E.Z., Bosco, D.A., Akke, M. and Kern, D. (2002). „Enzyme dynamics during catalysis”. Science 295: 1520-1523. PMID 11859194.
Literatura[uredi | uredi kod]
- 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.