Kinetics of precursor cleavage at the dibasic sites. Involvement of peptide dynamics
Détails
ID Serval
serval:BIB_CF8E78ED1F9C
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Kinetics of precursor cleavage at the dibasic sites. Involvement of peptide dynamics
Périodique
FEBS Letters
ISSN
0014-5793 (Print)
Statut éditorial
Publié
Date de publication
04/2002
Volume
516
Numéro
1-3
Pages
75-9
Notes
In Vitro
Journal Article --- Old month value: Apr 10
Journal Article --- Old month value: Apr 10
Résumé
The presence in the P'1 position relative to the LysArg doublet of either Phe, Tyr or Trp residues affects only pro-OT/Np(7-15) flexibility. This has a measurable effect on the dynamics of the peptide. Since the same modifications have a major influence on the K(m) and V(max) values of the peptide cleavage, these kinetic parameters should depend on the peptide substrate motions. Therefore, the primary kinetic contribution of substrate cleavage should arise from substrate dynamics rather than from the enzyme.
Mots-clé
Amino Acid Sequence
Arginine Vasopressin/chemistry/metabolism
Binding Sites
Circular Dichroism
Kinetics
Neurophysins/chemistry/metabolism
Oxytocin/*analogs & derivatives/chemistry/metabolism
Peptides/*chemistry/*metabolism
Protein Precursors/*chemistry/*metabolism
Protein Processing, Post-Translational
Spectrometry, Fluorescence
Pubmed
Web of science
Open Access
Oui
Création de la notice
28/01/2008 11:35
Dernière modification de la notice
20/08/2019 16:49