[Dialdehyde derivatives of purine mononucleotides: substrate properties and affinity modification of myosin ATPase].
It was demonstrated that the dialdehyde derivative of ATP is a good substrate for Ca-ATPase of heavy meromyosin (Km = (1.2-1.4) X 10(-4) M; V = VATP). At the same time, this compound can induce irreversible inhibition of the enzyme. Since oxo-ATP is rapidly hydrolyzed by myosin to form oxo-ADP, this inhibition is the result of the enzyme interaction with oxo-ADP. It was found that the kinetics of heavy meromyosin inhibition by oxo-ADP are typical of affinity modification; in this case ATP fully protects heavy meromyosin from the activity loss. Similar results on the irreversible inhibition of the ATPase activity under the action of oxo-ADP were obtained in the presence of myosin, heavy meromyosin, subfragment I and natural actomyosin and in the absence of bivalent cations, thus suggesting the modification of the active center of myosin ATPase.
Grishin
M N
MN
Kodentsova
V M
VM
Abdraimova
U A
UA
Nikolaeva
O P
OP
Petushkova
E V
EV
D000244:Adenosine Diphosphate / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000031:analogs & derivatives* / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D002850:Chromatography, Gel; D066298:In Vitro Techniques; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D051381:Rats; D013379:Substrate Specificity
C017199:2',3'-dialdehyde ATP; D000244:Adenosine Diphosphate; C018808:adenosine 5'-diphosphate 2',3'-dialdehyde; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases
Dial'degidnye proizvodnye purinovykh mononukleotidov: substratnye svoĭstva i affinnaia modifikatsiia miozinovoĭ ATPazy.