[Resistance to levomycetin and activity of several enzymes in Escherichia coli and the agent of plague].
The authors compared the activity of acetyl-CoA-synthetase and of the enzymes belonging to the group of asparaginic acid in levomycetin sensitive and resistant strains of Y. pestis and E. coli. There were revealed marked differences in the activity of aspartase, fumarase, synthetase and desamidase of L-asparagin, and also of the enzyme activated by acetate in the E. coli strains with plasmide resistance. Transmission of R-factor to the pestis was accompanied by decomposition of L-asparadein, formation of AC-CoA. At the same time transformation of L-asparaginic acid catalyzed by aspartase remained on the same low level in the sensitive pestis cultures and their variants with the R-factor. When the resistance was controlled by chromosomal resistance markers, the activity of the enzymes providing formation of L-asparagic acid, its amide and L-malic acid showed no significant change. In chromosomal type of resistance in the mutants of pestis and E. coli the acetyl-CoA-synthetase reaction was as a rule somewhat increased.
D000106:Acetate-CoA Ligase / Q000378:metabolism; D001215:Asparaginase / Q000378:metabolism; D001220:Aspartate Ammonia-Lyase / Q000378:metabolism; D001217:Aspartate-Ammonia Ligase / Q000378:metabolism; D002256:Carbonic Anhydrases / Q000378:metabolism; D002701:Chloramphenicol / Q000494:pharmacology*; D002875:Chromosomes; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000187:drug effects* / Q000201:enzymology; D010957:Plasmids; D000637:Transaminases / Q000378:metabolism; D015010:Yersinia pestis / Q000187:drug effects* / Q000201:enzymology
D002701:Chloramphenicol; D000637:Transaminases; D001215:Asparaginase; D002256:Carbonic Anhydrases; D001220:Aspartate Ammonia-Lyase; D000106:Acetate-CoA Ligase; D001217:Aspartate-Ammonia Ligase
Rezistentnost' k levomitsetinu i aktivnost' nekotorykh fementov u vozbuditaelia chumy i kishechnoĭ palochki