Evidence of substantial separation of the catalytic and allosteric sites of AMP nucleosidase.
D000241:Adenosine / Q000031:analogs & derivatives / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000494:Allosteric Regulation; D000495:Allosteric Site; D001395:Azotobacter / Q000201:enzymology*; D001665:Binding Sites; D004578:Electron Spin Resonance Spectroscopy; D007700:Kinetics; D008345:Manganese / Q000494:pharmacology; D009699:N-Glycosyl Hydrolases / Q000378:metabolism*; D013113:Spin Labels
D013113:Spin Labels; D000249:Adenosine Monophosphate; D008345:Manganese; D000255:Adenosine Triphosphate; C010223:N-methyladenosine; D009699:N-Glycosyl Hydrolases; C019699:AMP nucleosidase; D000241:Adenosine