Bailyes E M, Shennan K I, Seal A J, Smeekens S P, Steiner D F, Hutton J C, Docherty K
Department of Clinical Biochemistry, University of Cambridge, Addenbrookes Hospital, U.K.
Biochem J. 1992 Jul 15;285 ( Pt 2)(Pt 2):391-4. doi: 10.1042/bj2850391.
PC3, a mammalian homologue of the yeast subtilisin-like proteinase Kex2, was expressed in Xenopus oocytes and its activity was characterized. PC3 cleaved human proinsulin at one of the two dibasic sites (KTRR32 but not LQKR65). The specificity, inhibitor profile, pH optimum (5.5) and Ca(2+)-dependence (K0.5 = 2.5-3 mM) paralleled those of the insulin-granule type 1 endopeptidase activity, suggesting a role for PC3 in the conversion of prohormones.
PC3是酵母枯草杆菌蛋白酶样蛋白酶Kex2的哺乳动物同源物,它在非洲爪蟾卵母细胞中表达并对其活性进行了表征。PC3在两个双碱性位点之一(KTRR32,而非LQKR65)切割人胰岛素原。其特异性、抑制剂谱、最适pH(5.5)和钙依赖性(K0.5 = 2.5 - 3 mM)与胰岛素颗粒1型内肽酶活性相似,表明PC3在激素原转化中发挥作用。