In situ inactivation of E. coli uridylylation cycle is independent of the state of covalent modification of the components of the glutamine synthetase cascade.
D002463:Cell Membrane Permeability; D003902:Detergents / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology*; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D007700:Kinetics; D009713:Nucleotidyltransferases / Q000037:antagonists & inhibitors*; D011092:Polyethylene Glycols / Q000494:pharmacology; D006599:UDPglucose-Hexose-1-Phosphate Uridylyltransferase / Q000037:antagonists & inhibitors*; D014500:Uracil Nucleotides / Q000378:metabolism*; D014542:Uridine Monophosphate / Q000378:metabolism*
D003902:Detergents; D014500:Uracil Nucleotides; C017474:Lubrol WX; D011092:Polyethylene Glycols; D014542:Uridine Monophosphate; D009713:Nucleotidyltransferases; D006599:UDPglucose-Hexose-1-Phosphate Uridylyltransferase; D005974:Glutamate-Ammonia Ligase