title: Kinetics of precursor cleavage at the dibasic sites. Involvement of peptide dynamics.
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.
authors.affiliation: Université Denis Diderot, Laboratoire de Biologie Physico-chimique, 2 Place Jussieu, 75005, Paris, France.
authors.forename: Jean-Marie
authors.initials: JM
authors.lastname: Glandieres
authors.forename: Maud
authors.initials: M
authors.lastname: Hertzog
authors.forename: Noureddine
authors.initials: N
authors.lastname: Lazar
authors.forename: Noureddine
authors.initials: N
authors.lastname: Brakch
authors.forename: Paul
authors.initials: P
authors.lastname: Cohen
authors.forename: Bernard
authors.initials: B
authors.lastname: Alpert
authors.forename: Mohamed
authors.initials: M
authors.lastname: Rholam
mesh_terms: D000595:Amino Acid Sequence; D001127:Arginine Vasopressin / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002942:Circular Dichroism; D066298:In Vitro Techniques; D007700:Kinetics; D009481:Neurophysins / Q000737:chemistry / Q000378:metabolism; D010121:Oxytocin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011498:Protein Precursors / Q000737:chemistry* / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D013050:Spectrometry, Fluorescence
chemical_list: D009481:Neurophysins; D010455:Peptides; D011498:Protein Precursors; D001127:Arginine Vasopressin; D010121:Oxytocin; C046278:oxytocin, Gly-Lys-Arg-