29747-05-5Relevant articles and documents
Temperature-controlled NaI-mediated α-oxybenzoylation or oxyacylation-decarboxylation reactions of dimethyl malonate with carboxylic acids
Mao, Jincheng,Liu, Defu,Li, Yongming,Zhao, Jinzhou,Rong, Guangwei,Yan, Hong,Zhang, Guoqi
, p. 62 - 65 (2015)
A NaI-mediated α-functionalization of dimethyl malonate and its derivatives with carboxylic acids has been developed. Two different reaction routes based on the same substrates and reaction conditions by simply altering the reaction temperature have been
Chemoselective esterification and amidation of carboxylic acids with imidazole carbamates and ureas
Heller, Stephen T.,Sarpong, Richmond
supporting information; experimental part, p. 4572 - 4575 (2010/12/25)
Imidazole carbamates and ureas were found to be chemoselective esterification and amidation reagents. A wide variety of carboxylic acids were converted to their ester or amide analogues by a simple synthetic procedure in high yields.
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 (2007/10/03)
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.
