Allosteric regulation of the state of adenylylation of glutamine synthetase in permeabilized cell preparations of Escherichia coli. Studies of monocyclic and bicyclic interconvertible enzyme cascades, in situ.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000494:Allosteric Regulation; D002413:Cations, Divalent; D002463:Cell Membrane Permeability; D003201:Computers; D003568:Cytidine Monophosphate / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D005973:Glutamine / Q000494:pharmacology; D007656:Ketoglutaric Acids / Q000494:pharmacology; D007700:Kinetics; D009713:Nucleotidyltransferases / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000494:pharmacology; D014544:Uridine Triphosphate / Q000494:pharmacology
D002413:Cations, Divalent; D007656:Ketoglutaric Acids; D005973:Glutamine; C017474:Lubrol WX; D011092:Polyethylene Glycols; D000255:Adenosine Triphosphate; D009713:Nucleotidyltransferases; C020658:glutamine-synthetase adenylyltransferase; D005974:Glutamate-Ammonia Ligase; D003568:Cytidine Monophosphate; D014544:Uridine Triphosphate