[Interaction of acetyl-CoA-carboxylase from the rat liver with alkylating amides of ATP and ADP].
The interaction of 4-(N-chloroethyl-N-methylamino)-benzyl-gamma-amide ATP (I) and the corresponding beta-amide of ADP (II) with rat liver acetyl-CoA carboxylase was studied. Both analogs were shown to cause affinity modification of the enzyme. ATP and GoAS Ac protected the enzyme against inactivation. HCO3- increased the rate of carboxylase inactivation by analogs I and II (2.5- and 1.5-fold, respectively). The alkylating amides did not influence the rate of the bicarbonate-dependent [14C]-ADP-ATP exchange and inhibited the enzyme-catalyzed reaction of [14C]-CoAs Ac----CoAS Mal exchange, which testifies to the localization of the modified group in the CoAS Ac-binding site of the enzyme active center. Based on the affinity modification and analog size, it was found that the distance between the ATP- and CoAS Ac-binding sites of the enzyme active center can vary from 0.8 to 1.2 nm.
Amontov
S V
SV
Buneva
V N
VN
Rabinkov
A G
AG
Goriachenkova
E V
EV
D000103:Acetyl-CoA Carboxylase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000244:Adenosine Diphosphate / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D000477:Alkylating Agents / Q000378:metabolism / Q000494:pharmacology*; D000577:Amides / Q000378:metabolism / Q000494:pharmacology*; D000818:Animals; D001665:Binding Sites; D007700:Kinetics; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D051381:Rats
D000477:Alkylating Agents; D000577:Amides; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate; D008025:Ligases; D000103:Acetyl-CoA Carboxylase
Issledovanie vzaimodeĭstviia atsetil-CoA-karboksilazy pecheni krysy s alkiliruiushchimi amidami ATP i ADP.