5 Beta,14 beta-androstane-3 beta,14-diol binds to the digitalis receptor site on Na/K-ATPase.
5 beta,14 beta-Androstane-3 beta,-14-diol, the lead (minimum) structure in digitalis compounds, shows the same characteristics of interaction with Na/K-ATPase as ordinary digitalis compounds judged by the following six criteria: (I) shape of the concentration-inhibition curves, (II) species differences in affinity for the enzyme, (III) apparent competition with K+, (IV) competition with digitoxigenin for binding to the enzyme, (V) stabilization of phosphoenzyme formed from ATP, and (VI) enhancement of phosphorylation from orthophosphate.
Schönfeld
W
W
Central Institute of Molecular Biology, Academy of Sciences, G.D.R., Berlin.
Menke
K H
KH
Schönfeld
R
R
Repke
K R
KR
D015113:Androstane-3,17-diol / Q000031:analogs & derivatives / Q000378:metabolism* / Q000494:pharmacology; D000732:Androstanols / Q000378:metabolism*; D001665:Binding Sites; D001667:Binding, Competitive; D002540:Cerebral Cortex / Q000201:enzymology; D004071:Digitalis Glycosides / Q000378:metabolism* / Q000494:pharmacology; D006801:Humans; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D013329:Structure-Activity Relationship
D000732:Androstanols; D004071:Digitalis Glycosides; D015113:Androstane-3,17-diol; C046550:androstane-3,14-diol; D000254:Sodium-Potassium-Exchanging ATPase