Green D P
Med Hypotheses. 1984 Sep;15(1):47-59. doi: 10.1016/0306-9877(84)90007-0.
A number of lines of evidence suggest that the polypeptide prohormone converting enzyme is a trypsin-like serine protease. A model is proposed in which the converting enzyme is activated from an inactive zymogen during secretion. Converting enzyme then activates co-secreted prohormone proteolytically. An important feature of the model lies in the geometry of the secretory granule immediately after exocytosis. It is suggested that initially diffusion of the granule contents is limited enough to allow extensive proteolysis to occur. Conversion of prohormone to hormone is terminated by diffusion of converting enzyme and prohormone from the site of release.
大量证据表明，多肽激素原转化酶是一种类胰蛋白酶丝氨酸蛋白酶。本文提出了一个模型，即在分泌过程中，转化酶从无活性的酶原被激活。然后，转化酶通过蛋白水解作用激活共同分泌的激素原。该模型的一个重要特征在于胞吐作用刚发生后分泌颗粒的几何形状。有人认为，最初颗粒内容物的扩散受到足够限制，从而允许广泛的蛋白水解作用发生。激素原向激素的转化通过转化酶和激素原从释放部位的扩散而终止。
