[Functionally different states of the "hydrophobic pocket" of the myosin ATPase center].
The influence of an increased temperature (39 degrees C) on a denaturation of 50 kDa-fragment of myosin subfragment 1 was studied in the presence of different nucleoside triphosphates (NTP) and nucleoside diphosphates (NDP). The degree of the denaturation was appreciated evaluated from its trypsinolysis depth. According to their protective influence NTP and NDP were shown to arrange in lines ATP greater than or equal to CTP greater than UTP greater than GTP and ADP greater than GDP greater than CDP greater than UDP, correspondingly. The results received and the literature data allow to suggest that there are at least two states of ATPase site hydrophobic pocket, one of which in responsible for sharp ATPase reaction slowing-down on the stage of macroergic bonding splitting.
Babiĭchuk
E B
EB
Filenko
A M
AM
D000244:Adenosine Diphosphate / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D003565:Cytidine Diphosphate / Q000378:metabolism; D003570:Cytidine Triphosphate / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006153:Guanosine Diphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D013835:Thiamine Pyrophosphate / Q000378:metabolism; D013838:Thiamine Triphosphate / Q000378:metabolism; D014530:Uridine Diphosphate / Q000378:metabolism; D014544:Uridine Triphosphate / Q000378:metabolism
D006153:Guanosine Diphosphate; D013838:Thiamine Triphosphate; D014530:Uridine Diphosphate; D000244:Adenosine Diphosphate; D003565:Cytidine Diphosphate; D003570:Cytidine Triphosphate; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D009218:Myosins; D013835:Thiamine Pyrophosphate; D014544:Uridine Triphosphate
Funktsional'no razlichnye sostoianiia "gidrofobnogo karmana" ATP-aznogo tsentra miozina.