Kinetics of precursor cleavage at the dibasic sites. Involvement of peptide dynamics

Details

Serval ID
serval:BIB_CF8E78ED1F9C
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Kinetics of precursor cleavage at the dibasic sites. Involvement of peptide dynamics
Journal
FEBS Letters
Author(s)
Glandieres  J. M., Hertzog  M., Lazar  N., Brakch  N., Cohen  P., Alpert  B., Rholam  M.
ISSN
0014-5793 (Print)
Publication state
Published
Issued date
04/2002
Volume
516
Number
1-3
Pages
75-9
Notes
In Vitro
Journal Article --- Old month value: Apr 10
Abstract
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.
Keywords
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
Yes
Create date
28/01/2008 10:35
Last modification date
20/08/2019 15:49
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