Kinetics of precursor cleavage at the dibasic sites. Involvement of peptide dynamics.
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.
Glandieres
Jean-Marie
JM
Université Denis Diderot, Laboratoire de Biologie Physico-chimique, 2 Place Jussieu, 75005, Paris, France.
Hertzog
Maud
M
Lazar
Noureddine
N
Brakch
Noureddine
N
Cohen
Paul
P
Alpert
Bernard
B
Rholam
Mohamed
M
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
D009481:Neurophysins; D010455:Peptides; D011498:Protein Precursors; D001127:Arginine Vasopressin; D010121:Oxytocin; C046278:oxytocin, Gly-Lys-Arg-