151434-07-0Relevant articles and documents
Inhibition of peptidylglycine α-amidating monooxygenase by exploitation of factors affecting the stability and ease of formation of glycyl radicals
Barratt, Brendon J. W.,Easton, Christopher J.,Henry, David J.,Li, Iris H. W.,Radom, Leo,Simpson, Jamie S.
, p. 13306 - 13311 (2004)
Peptidylglycine α-amidating monooxygenase catalyzes the biosynthesis of peptide hormones through radical cleavage of the C-terminal glycine residues of the corresponding prohormones. We have correlated ab initio calculations of radical stabilization energies and studies of free radical brominations with the extent of catalysis displayed by peptidylglycine α-amidating monooxygenase, to identify classes of inhibitors of the enzyme. In particular we find that, in closely related systems, the substitution of glycolate for glycine reduces the calculated radical stabilization energy by 34.7 kJ mol -1, decreases the rate of bromination with N-bromosuccinimide at reflux in carbon tetrachloride by a factor of at least 2000, and stops catalysis by the monooxygenase, while maintaining binding to the enzyme.
Intramolecular Participation by a Neighboring Amide Group in the Hydrolysis of N-Acylimidazoles
Kogan, Robert L.,Fife, Thomas H.
, p. 5229 - 5232 (1984)
Rate constants have been determined for the disappearance of the N-acylimidazole derivatives of N-acetylphenylalanine and N-acetylvaline in H2O at 30 deg C.The pH-rate constant profiles are characterized by large pH-independent regions.These reactions are
