Denault J B, Leduc R
Department of Pharmacology, Faculty of Medicine, Université de Sherbrooke, Québec, Canada.
FEBS Lett. 1996 Jan 29;379(2):113-6. doi: 10.1016/0014-5793(95)01487-x.
One of the most exciting breakthroughs of the 90's in the fields of biochemistry, cell biology and neuroendocrinology is the identification of a novel family of proteolytic enzymes called mammalian subtilisin-like convertases. This family is comprised so far of seven distinct endoproteases responsible for the proteolytic excision of biologically active polypeptides from inactive precursor proteins. Six years after the initial observation of a structural conservation between a characterized yeast enzyme (kexin) and a human gene product (furin), it is now well accepted that one of these convertases, furin, has the enzymatic capabilities to efficiently and correctly process a great variety of precursors. Furin's ability to cleave precursors within both the exocytic and endocytic pathways will require sustained efforts in order to delineate all of its physiological roles.
20世纪90年代在生物化学、细胞生物学和神经内分泌学领域最令人兴奋的突破之一，是发现了一个新的蛋白水解酶家族，称为哺乳动物枯草杆菌蛋白酶样转化酶。到目前为止，这个家族由七种不同的内切蛋白酶组成，它们负责从无活性的前体蛋白中蛋白水解切除生物活性多肽。在最初观察到一种已鉴定的酵母酶（克新）和一种人类基因产物（弗林蛋白酶）之间存在结构保守性六年之后，现在人们普遍认为这些转化酶之一，即弗林蛋白酶，具有有效且正确处理多种前体蛋白的酶促能力。弗林蛋白酶在胞吐和胞吞途径中切割前体蛋白的能力，需要持续的努力才能明确其所有的生理作用。
