[Adenylate cyclase from rabbit heart: substrate binding site].
The effects of 17 ATP analogs on the solubilized rabbit heart adenylate cyclase were studied. The triphosphate chain, position 8 of the adenine base and the ribose residue of the ATP molecule were modified. Despite the presence of the alkylating groups in two former types of the analogs tested, no covalent blocking of the active site of the enzyme was observed. Most of the compounds appeared to be competitive reversible inhibitors. The kinetic data confirmed the importance of the triphosphate chain for substrate binding in the active site of adenylate cyclase. (Formula: See Text) The inhibitors with different substituents in position 8 of the adenine base had a low affinity for the enzyme. The possible orientation of the triphosphate chain and the advantages of anti-conformation of the ATP molecule for their binding in the active site of adenylate cyclase are discussed.
D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D009206:Myocardium / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D013329:Structure-Activity Relationship
D000255:Adenosine Triphosphate; D000262:Adenylyl Cyclases
Adenilattsiklaza iz cerdtsa krolika: issledovanie substratsviazyvaiushchego uchastka.