[Phosphate group donors for neomycin inactivation by resistant microorganism strains].
The substrate specificity of aminoglycoside phosphotransferases isolated from 3 strain of E. coli and purified was studied. All pure enzymes phosphorilated neomycin, paromomycin, lividomycin, neamine, ribostamycin, kanamycins A and B. Only ATP was the donor of the phosphate groups in these reactions, while in the non-purified extracts GTP but not UTP or CTP served as the donor of the phosphate group for inactivation of neomycin. The substrate specificity indicated that the above enzymes were aminoglycoside-3(1)-phosphotransferases. Inactivation of neomycin with the use of the phosphate group of phosphoenolpiruvate as the donor in the non-purified enzymatic preparations of the neomycin-resistant strains of E. coli and Pseudomonas was not observed.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000617:Aminoglycosides; D004352:Drug Resistance, Microbial; D004789:Enzyme Activation; D004926:Escherichia coli / Q000201:enzymology; D009355:Neomycin / Q000037:antagonists & inhibitors*; D009943:Organophosphorus Compounds / Q000378:metabolism*; D010728:Phosphoenolpyruvate / Q000378:metabolism; D010770:Phosphotransferases / Q000378:metabolism; D011549:Pseudomonas / Q000201:enzymology; D013379:Substrate Specificity
D000617:Aminoglycosides; D009943:Organophosphorus Compounds; D010728:Phosphoenolpyruvate; D000255:Adenosine Triphosphate; D010770:Phosphotransferases; D009355:Neomycin
Donory fosfatnykh grupp dlia inaktivatsii neomitsina rezistentnymi shtammami mikroorganizmov.