Peptidilprolilna izomeraza

Peptidilprolilna izomeraza
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
Pretraga
PMC articles
PubMed articles
NCBI Protein search

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) ⇌ {\displaystyle \rightleftharpoons } 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

  1. ↑ 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. 
  2. ↑ 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. 
  3. ↑ 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. 
  4. ↑ 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. 
  5. ↑ 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. 
  6. ↑ Fischer, G. (1994). „Peptidyl-prolyl cis/trans isomerases and their effectors”. Angew. Chem. Int. Ed. Engl. 33: 1415-1436. 
  7. ↑ 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. 
  8. ↑ Eisenmesser, E.Z., Bosco, D.A., Akke, M. and Kern, D. (2002). „Enzyme dynamics during catalysis”. Science 295: 1520-1523. PMID 11859194. 

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. 

Spoljašnje veze

  • MeSH Peptidylprolyl+isomerase
  • p
  • r
  • u
TemeTipovi
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