Malonylcoenzyme a models. Part 1. E1cB (keten) Pathway for acyl transfers of malonic acid thiolmonoesters including S-malonylcoenzyme A

Publisher Website
Google Scholar
Abstract
The aminolysis of a series of malonate thiolmonoesters (HO2CCH2COSR) has been studied kinetically at 25 °C. No indication of substrate ionisation was observed for the S-4-chlorophenyl and S-phenyl esters up to 0.45M-sodium hydroxide. Morpholinolysis showed saturation kinetics, i.e. the observed pseudo-first-order rate constant became insensitive to morpholine concentration at higher morpholine concentrations. This behaviour was analysed in terms of the rate equation kobs=kmax.[B]/(K+[B]), where kmax. is the limiting rate constant at higher buffer (B) concentrations and K the concentration of buffer required for kobs= 0.5 kmax. Saturation aminolysis was also observed for S-malonylcoenzyme A. Arrhenius parameters were determined for the above kinetic parameters (kmax., K, kmax./K) for the S-benzyl ester. Trapping experiments with aniline showed that rate-determining and product-determining steps differed. The results were interpreted in terms of an intermediate keten formed from the ester dianion (–O2CCHCOSR). However, to explain leaving-group dependences of kmax., K, etc., a degree of leaving-group protonation in the transition-state had to be invoked, although mechanisms involving the zwitterion-anion [–O2CCH·COS(H)R] could be excluded.

This publication has 0 references indexed in Scilit: