Kalikrein

Kalikreini su podgrupa serinskih proteaza, enzima koji imaju sposobnost razlaganja peptidnih veza u proteinima. Kod ljudi, kalikrein plazme[1][2][3][4][5] (KLKB1) nema poznatih homologa, dok tkivne kalikreinu srodne peptidaze (KLKs) kodiraju familiju od petnaest blisko srodnih serinskih proteaza. Ti geni su locirani na hromozomu 19q13, i formiraju najveći kluster susednih proteaza u ljudskom genomu. Kalikreini su odgovorni za koordinaciju raznih fizioloških funkcija uključujući krvni pritisak, utečnjavanje semena i deskvamaciju kože.

Reference

  1. Heimark, R.L. and Davie, E.W. (1981). „Bovine and human plasma prekallikrein”. Methods Enzymol. 80: 157-172. PMID 6918767. 
  2. McRae, B.J., Kurachi, K., Heimark, R.L., Fujikawa, K., Davie, E.W. and Powers, J.C. (1981). „Mapping the active sites of bovine thrombin, factor IXa, factor Xa, factor XIa, factor XIIa, plasma kallikrein, and trypsin with amino acid and peptide thioesters: development of new sensitive substrates”. Biochemistry 20: 7196-7206. PMID 6976185. 
  3. Silverberg, M. and Kaplan, A.P. (1988). „Prekallikrein”. Methods Enzymol. 163: 85-95. PMID 3237096. 
  4. Seidah, N.G., Ladenheim, R., Mbikay, M., Hamelin, J., Lutfalla, G., Rougeon, F., Lazure, C. and Chrétien, M. (1989). „The cDNA structure of rat plasma kallikrein”. DNA 8: 563-574. PMID 2598771. 
  5. Tsuda, Y., Teno, N., Okada, Y., Wanaka, K., Bohgaki, M., Hijikata-Okunomiya, A., Okamoto, U., Naito, T. and Okamoto, S. (1989). „Synthesis of tripeptide chloromethyl ketones and examination of their inhibitory effects on plasmin and plasma kallikrein”. Chem. Pharm. Bull. 37: 3108-3111. PMID 2534361. 

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. 

Vidi još

  • Kalikrein plazme, enzim
  • Kalikrein renalnog tkiva, enzim

Spoljašnje veze

  • MEROPS onlajn baza podataka o peptidazama i njihovim inhibitorima: S01.212 Arhivirano 2020-05-27 na Wayback Machine-u
  • MeSH Kallikreins
  • p
  • r
  • u
Proteini: enzimi
Teme
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
Tipovi
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