Kinetics and mechanism of the cleavage of the peptide bond next to asparagine.
The spontaneous cleavage reaction of the tetra-peptide Piv-Gly Asn-Sar-Gly-NHtBu to the C-terminal dipeptide and N-terminal succinimide dipeptide proceeds through pre-equilibrium deprotonation of the amide group of the asparagine side chain, followed by intramolecular nucleophilic attack of nitrogen on the peptide carbonyl carbonyl carbon atom. General acid-catalyzed breakdown of the intermediate then gives the products. According to this mechanism, the reaction rate strongly increases with pH and buffer concentration.
Centro di studio di Biocristallografia, CNR, Napoli, Italy.
S
S
Capasso
L
L
Mazzarella
G
G
Sorrentino
G
G
Balboni
A J
AJ
Kirby
D001216:Asparagine / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D009842:Oligopeptides / Q000737:chemistry*; D019154:Protein Splicing; D013388:Succinimides / Q000737:chemistry
D009842:Oligopeptides; D013388:Succinimides; C103991:pivaloyl-glycyl-asparaginyl-sarcosyl-N-(t-butyl)glycinamide; C032620:succinimide; D001216:Asparagine