title: Melittin interactions with adenylate cyclase.
abstract: Melittin, a basic polypeptide from bee venom, inhibits basal and thyrotropin-stimulated adenylate cyclase of beef thyroid membranes with a Ki approximately 10 micron. Although this property resides in the basic C-terminal and not the N-terminal portion of the molecule, inhibition is due primarily to its detergent-like nature rather than charge effects. There is also a small enhancing effect of both basal and thyrotropin-stimulated adenylate cyclase of 0.3-3 micron melittin.
mesh_terms: D000262:Adenylyl Cyclases / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D007700:Kinetics; D008555:Melitten / Q000494:pharmacology*; D011189:Potassium Chloride / Q000494:pharmacology; D011485:Protein Binding; D013961:Thyroid Gland / Q000201:enzymology*; D013972:Thyrotropin / Q000494:pharmacology; D014688:Venoms / Q000494:pharmacology*
chemical_list: D014688:Venoms; D008555:Melitten; D011189:Potassium Chloride; D013972:Thyrotropin; D000262:Adenylyl Cyclases