Protease inhibitor controls prophenoloxidase activation in Manduca sexta.
Prophenoloxidase from the hemolymph of tobacco hornworm Manduca sexta can be activated by a specific activating enzyme found in the cuticle. Inhibition studies with benzamidine, diisopropyl phosphofluoridate and p-nitrophenyl-p'-guanidinobenzoate indicate that the activating enzyme is a trypsin-like serine protease. An endogenous protease inhibitor, isolated from the hemolymph of Manduca larvae, inhibits the prophenoloxidase activation mediated by this enzyme. These results indicate that the probable physiological role of endogenous protease inhibitor is to control the undesired activation of prophenoloxidase in the hemolymph.
D000818:Animals; D002384:Catalysis; D004156:Catechol Oxidase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002845:Chromatography / Q000379:methods; D010450:Endopeptidases / Q000378:metabolism; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006458:Hemolymph / Q000032:analysis; D007915:Lepidoptera / Q000201:enzymology*; D009036:Moths / Q000201:enzymology*; D011480:Protease Inhibitors / Q000502:physiology*; D012697:Serine Endopeptidases
D004792:Enzyme Precursors; D011480:Protease Inhibitors; C038451:pro-phenoloxidase; D004156:Catechol Oxidase; D010450:Endopeptidases; D012697:Serine Endopeptidases