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.
Capasso
S
S
Centro di studio di Biocristallografia, CNR, Napoli, Italy.
Mazzarella
L
L
Sorrentino
G
G
Balboni
G
G
Kirby
A J
AJ
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