The identification of prolyl endopeptidase in bovine lenses: a preliminary report.
A new neutral endopeptidase having the properties of prolyl endopeptidase was detected in bovine lenses. The enzyme hydrolyzed the prolyl bond in the newly-developed fluorogenic substrate, t-butyloxycarbonyl-Arg-Pro-2-NNap, optimally at pH 8 and 37 degrees. The Km value was estimated to be 0.033 mM. An approximately 4-fold purification was achieved. DFP completely inhibited the hydrolysis of Boc-Arg-Pro-2-NNap by the endopeptidase.
D000818:Animals; D002417:Cattle; D004151:Dipeptides / Q000378:metabolism; D010450:Endopeptidases / Q000032:analysis* / Q000494:pharmacology; D005456:Fluorescent Dyes; D066298:In Vitro Techniques; D007908:Lens, Crystalline / Q000201:enzymology*; D000085822:Prolyl Oligopeptidases; D012697:Serine Endopeptidases
D004151:Dipeptides; D005456:Fluorescent Dyes; C041322:tert-butyloxycarbonyl-arginylproline-2-naphthylamide; D010450:Endopeptidases; D012697:Serine Endopeptidases; D000085822:Prolyl Oligopeptidases