木瓜蛋白酶S1'亚位点的特异性。
The specificity of the S1' subsite of papain.
作者信息
Alecio M R, Dann M L, Lowe G
出版信息
Biochem J. 1974 Aug;141(2):495-501. doi: 10.1042/bj1410495.
The specificity of the S(1)' subsite of the proteolytic enzyme papain was investigated by studying the effect of l-alpha-amino acid amides on the enzyme-catalysed hydrolysis of N-benzyloxycarbonylglycine p-nitrophenyl ester and by determining the kinetic parameters for the enzyme-catalysed hydrolysis of some N-benzyloxycarbonylglycyl-l-amino acid amides. These studies showed that the S(1)' subsite has a predilection for hydrophobic residues, in particular l-leucine and l-tryptophan. The specificity for these residues is manifest in both the binding and acylation steps. N-Benzyloxycarbonylglycine amide is not hydrolysed under comparable conditions, indicating that the amide group adjacent to and on the C-terminal side of the peptide bond about to be cleaved makes an important contribution to the rate of the papain-catalysed hydrolysis of peptides.
通过研究L-α-氨基酸酰胺对木瓜蛋白酶催化的N-苄氧羰基甘氨酸对硝基苯酯水解的影响，并测定一些N-苄氧羰基甘氨酰-L-氨基酸酰胺的酶催化水解的动力学参数，研究了蛋白水解酶木瓜蛋白酶S(1)'亚位点的特异性。这些研究表明，S(1)'亚位点对疏水残基具有偏好性，特别是L-亮氨酸和L-色氨酸。这些残基的特异性在结合和酰化步骤中均有体现。在可比条件下，N-苄氧羰基甘氨酸酰胺不被水解，这表明即将被裂解的肽键C端侧相邻的酰胺基团对木瓜蛋白酶催化的肽水解速率有重要贡献。
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