HERRIOTT R M
J Gen Physiol. 1962 Mar;45(4)Pt 2(4):57-76.
Evidence relating to the structure and properties of swine pepsinogen and pepsin has been reviewed and used to suggest a tentative two dimensional picture of the skeleton of these two proteins. When pepsinogen, a folded single peptide chain, is converted to pepsin, there is a profound change in the physical and chemical properties of the protein. In an as yet unknown manner, except that it is initiated by a peptic cleavage of the protein chain, a single enzymic site is formed. This site is made up, quite probably, of the secondary carboxyl group of glutamic acid or of aspartic acid and a tyrosine phenol group in close proximity so that they can form hydrogen or hydrophobic bonds with the substrate in some unique manner that permits hydrolysis to occur at an accelerated rate.
有关猪胃蛋白酶原和胃蛋白酶的结构与特性的证据已被综述,并用于推测这两种蛋白质骨架的二维示意图。胃蛋白酶原是一种折叠的单肽链,当它转化为胃蛋白酶时,蛋白质的物理和化学性质会发生深刻变化。除了由蛋白质链的消化性裂解引发外,以一种尚不清楚的方式形成了一个单一的酶活性位点。这个位点很可能由谷氨酸或天冬氨酸的仲羧基和紧邻的酪氨酸酚基组成,这样它们就能以某种独特的方式与底物形成氢键或疏水键,从而使水解以加速的速率发生。