Magnolizin

Magnolizin
Identifikatori
EC broj 3.4.24.62
CAS broj 162875-09-4
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

Magnolizin (EC 3.4.24.62, prooksitocin/neurofizin konvertaza, prooksifizinska proteinaza, prooksitocinska konvertaza) je enzim.[1][2][3][4][5] Ovaj enzim katalizuje sledeću hemijsku reakciju

Hidroliza polipeptida sa Arg ili Lys u P1 i P2, e.g. hidroliza prooksitocina u -Lys-Arg-Ala-Val-. Dalja specifičnos je zavisna od organizacije beta-zaokret-alfa-heliksa sa devet ili više ostataka koji sadrže parove baznih aminokiselina blizo centra

Ova endopeptidaza je prisutna u goveđoj hipofizi.

Reference

  1. Clamagirand, C., Creminon, C., Fahy, C., Boussetta, H. and Cohen, P. (1987). „Partial purification and functional properties of an endoprotease from bovine neurosecretory granules cleaving proocytosin/neurophysin peptides at the basic amino acid doublet”. Biochemistry 26: 6018-6023. PMID 2825769. 
  2. Créminon, C., Rholam, M., Boussetta, H., Marrakchi, N. and Cohen, P. (1988). „Synthetic peptide substrates as models to study a pro-ocytocin/neurophysin converting enzyme”. J. Chromatogt. 440: 439-448. PMID 3042797. 
  3. Brakch, N., Boussetta, H., Rholam, M. and Cohen, P. (1989). „Processing endoprotease recognizes a structural feature at the cleavage site of peptide prohormones. The pro-ocytocin/neurophysin model”. J. Biol. Chem. 264: 15912-15916. PMID 2674120. 
  4. Plevrakis, I, Créminon, C., Clamagirand, C., Brakch, N., Rholam, M. and Cohen, P. (1989). „Proocytocin/neurophysin convertase from bovine neurohypophysis and corpus luteum secretory granules: complete purification, structure-function relationships, and competitive inhibitor”. Biochemistry 28: 2705-2710. PMID 2659078. 
  5. Guillou, M.D., Camier, M. and Clamagirand, C. (1994). „Evidence for the presence of pro-oxytocin/neurophysin converting enzyme in the human ovary”. J. Endocrinol. 142: 345-352. PMID 7931007. 

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

  • 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