魚類幽門垂プロティナーゼに関する研究-IV : サバ幽門垂プロティナーゼによるN-ベンゾイル-L-アルギニンアミドの分解反応の速度論

概要

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Kinetic studies have been made on the hydrolytic reactions of synthetic peptide catalyzed by purified mackerel proteinase. The kinetic constant, the apparent Michaelis constant Km and the apparent maximal velocity Vmax, were determined for the hydrolysis of Nα-benzoyl-L-arginineamide. It is important to note that the factors which influence the velocity of enzyme reactions may be produced by either one of the following: by an effect on the formation, or an effect on the breakdown, of the enzyme-substrate complex. The Michaelis constant Km and the maximal velocity Vmax were found to be 0.79 X 10-3 M and 27.7 M per mole of enzyme per min. respectively, at pH 9.0 and 35°C. The activation energy for the mackerel proteinase is calculated to be 6.5 K cal. Judging from the results of kinetic analysis, it was proposed that, combined with substrate in the activated complex, a sort of ES-complex is readily formed by the mackerel proteinase.
公益社団法人日本水産学会の論文