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A conformational mechanism for formation of a dead-end complex by the sarcoplasmic reticulum ATPase with thapsigargin
1992
Journal of Biological Chemistry
Thapsigargin (TG), a plant sesquiterpene lactone extract, interacts tightly with the sarcoplasmic reticulum (SR) Ca2+ transport ATPase yielding a 1:1 stoichiometric complex. In addition to inhibiting steady state enzyme activity, TG can be shown to inhibit two individual partial reactions of the ATPase cycle (i.e. Ca2+ binding in the absence of ATP and enzyme phosphorylation by Pi in the absence of Ca2+) even when these reactions are studied separately without interdependence. As the two
pmid:1530936
fatcat:cnu65frohbdctnyya2zy3jwrrq