Studies on the reaction mechanism of adenosine triphosphate: glutamine synthetase adenylyltransferase from Escherichia coli B. Conformational changes elicited by effectors and substrates: reactivity of sulfhydryl groups.
D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D000494:Allosteric Regulation; D001565:Benzoates; D004220:Disulfides; D004926:Escherichia coli / Q000201:enzymology*; D005246:Feedback; D005974:Glutamate-Ammonia Ligase / Q000037:antagonists & inhibitors; D005973:Glutamine; D005994:Glycerophosphates; D006863:Hydrogen-Ion Concentration; D007656:Ketoglutaric Acids; D007700:Kinetics; D008274:Magnesium; D009574:Nitro Compounds; D009713:Nucleotidyltransferases; D011487:Protein Conformation; D013438:Sulfhydryl Compounds
D001565:Benzoates; D004220:Disulfides; D005994:Glycerophosphates; D007656:Ketoglutaric Acids; D009574:Nitro Compounds; D013438:Sulfhydryl Compounds; D005973:Glutamine; D000249:Adenosine Monophosphate; D000255:Adenosine Triphosphate; D009713:Nucleotidyltransferases; D005974:Glutamate-Ammonia Ligase; D008274:Magnesium