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Kinetics of precursor cleavage at the dibasic sites
Author(s) -
Glandieres Jean-Marie,
Hertzog Maud,
Lazar Noureddine,
Brakch Noureddine,
Cohen Paul,
Alpert Bernard,
Rholam Mohamed
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02505-x
Subject(s) - cleavage (geology) , peptide , chemistry , kinetics , substrate (aquarium) , stereochemistry , dibasic acid , kinetic energy , enzyme , biochemistry , biology , organic chemistry , physics , paleontology , ecology , quantum mechanics , fracture (geology)
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.