Kazanskaia N F, Kost O A
Biokhimiia. 1982 May;47(5):834-41.
The inhibition by N-benzoyl-L-arginine of subtilisin-catalyzed hydrolysis of various substrates was investigated. Study of combined hydrolysis of these substrates revealed the existence of two productive binding sites in the subtilisin 72 molecule. The type of substrate adsorption depends on the nature of the acyl moiety of the molecule and on the nature of the split-off group. The N-acetyl-L-tyrosine ethyl ester and N-benzoyl-L-citrulline methyl ester are bound at the same adsorption site (A), while N-cinnamoyl imidazole and N-acetyl-L-valine methyl ester are found at another adsorption site (B); N-benzoyl-L-alanine methyl ester can be adsorbed both at site A and at site B. However, substitution of the split-off group in the substrates previously adsorbed at site B by the p-nitrophenyl group causes their transfer to site A.
研究了N-苯甲酰-L-精氨酸对枯草杆菌蛋白酶催化各种底物水解的抑制作用。对这些底物联合水解的研究表明，枯草杆菌蛋白酶72分子中存在两个活性结合位点。底物吸附的类型取决于分子酰基部分的性质和裂解基团的性质。N-乙酰-L-酪氨酸乙酯和N-苯甲酰-L-瓜氨酸甲酯结合在同一吸附位点（A），而N-肉桂酰咪唑和N-乙酰-L-缬氨酸甲酯则在另一个吸附位点（B）被发现；N-苯甲酰-L-丙氨酸甲酯既可以吸附在位点A，也可以吸附在位点B。然而，将先前吸附在位点B的底物中的裂解基团用对硝基苯基取代会导致它们转移到位点A。
