165062-70-4Relevant academic research and scientific papers
Palladium Catalysis in the Intramolecular Carbene C–H Insertion of α-Diazo-α-(methoxycarbonyl)acetamides to Form β-Lactams
Solé, Daniel,Pérez-Janer, Ferran,Bennasar, M.-Llu?sa,Fernández, Israel
, p. 4446 - 4455 (2018/09/11)
The intramolecular carbene C–H insertion of α-diazo-α-(methoxycarbonyl)acetamides leading to β-lactams is effectively catalyzed by palladium complexes. It is found that although Pd0 catalysts typically produce mixtures of β-lactams together wit
Substituted aryl malonamates as new serine β-lactamase substrates: Structure-activity studies
Adediran,Cabaret,Lohier,Wakselman,Pratt
experimental part, p. 282 - 291 (2010/04/05)
A series of substituted aryl malonamates have been prepared. These compounds are analogues of aryl phenaceturates where the amido side chain has been replaced by a retro-amide. Like the phenaceturates, these compounds are substrates of typical class A and class C β-lactamases, particularly of the latter, and of soluble DD-peptidases. The effect of substituents α to the ester carbonyl group on turnover by these enzymes is similar to that in the phenaceturates. On the other hand, N-alkylation of the side chain amide of malonamates, but not of phenaceturates, retains the susceptibility of the compounds to hydrolysis by β-lactamases. This reactivity is not enhanced, however, by bridging the amide nitrogen and Cα atoms. A phosphonate analogue of the malonamates was found to be an irreversible inhibitor of the β-lactamases. These results, therefore, provide further evidence for the covalent access of compounds bearing retro-amide side chains to the active sites of β-lactam-recognizing enzymes.
