140-77-2Relevant articles and documents
Pancrazio
, p. 145 (1957)
Synthetic method of acid compound
-
Paragraph 0028-0033; 0041, (2020/08/25)
The invention belongs to the field of organic synthesis, and particularly relates to a synthetic method of an acid compound. An acid anhydride compound and an alkyl bromide or a functionalized alkyl bromide are subjected to a cross-electrophilic coupling reaction to synthesize an acid compound, so that the application of the alkyl bromide in the cross-electrophilic coupling reaction is expanded, and a novel non-traditional method for chemically and selectively constructing a carbon-carbon bond through a decarburization process is provided. The synthesis method is simple, economic, green and environment-friendly, and has wider applicability or is suitable for large-scale production.
Structure activity studies with xenobiotic substrates using carboxylesterases isolated from Arabidopsis thaliana
Cummins, Ian,Landrum, Marie,Steel, Patrick G.,Edwards, Robert
, p. 811 - 818 (2008/03/13)
Carboxylesterases (CXEs) catalyse the hydrolysis of xenobiotics and natural products radically altering their biological activities. Whereas the substrate selectivity of animal CXEs, such as porcine liver esterase (PLE) have been well studied, the respective enzymes in plants have yet to be defined and their activities determined. Using Arabidopsis thaliana (At) as a source, five representative members of the α/β hydrolase AtCXE family of proteins have been cloned, expressed and the purified recombinant proteins assayed for esterase activity with xenobiotic substrates. Two members, AtCXE5 and AtCXE18 were found to be active carboxylesterases, though AtCXE5 proved to be highly unstable as a soluble protein. AtCXE18 and the previously characterised S-formylglutathione hydrolase from Arabidopsis (AtSFGH) were assayed against a series of esters based on methylumbelliferone in which the acyl moiety was varied with respect to size and conformation. The same series was used to assay crude esterase preparation from Arabidopsis plants and the results compared with those obtained with the commonly used PLE. With straight chain esters, AtCXE18 behaved like PLE, but the Arabidopsis hydrolases proved less tolerant of branched chain acyl components than the mammalian enzyme. While none of the enzyme preparations accurately reflected all the activities determined with crude Arabidopsis protein extracts, the plant enzymes proved more useful than PLE in predicting the hydrolysis of the more sterically constrained esters.