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首页> 外文期刊>Bulletin of the Chemical Society of Japan >Relationship between the Hydrophobicity of Dipeptides and the Michaelis-Menten Constant K_m of Their Hydrolysis by Carboxypeptidase-Y and Carboxypeptidase-A
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Relationship between the Hydrophobicity of Dipeptides and the Michaelis-Menten Constant K_m of Their Hydrolysis by Carboxypeptidase-Y and Carboxypeptidase-A

机译:肽的疏水性与羧肽酶-Y和羧肽酶-A水解的Michaelis-Menten常数K_m之间的关系

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摘要

The enzymatic hydrolysis of dipeptides by carboxypeptidase-Y and carboxypeptidase-A was investigated.In the enzymatic hydrolysis of the dipeptides,a good linear relationship(r=0.997 and 0.999)was found between the Michaelis-Menten constant(K_m)and the hydrophobicity of the substrates evaluated from relative elution volume in reversed-phase HPLC.The correlation suggests that the hydrophobicity of the C-terminal amino acid is a major factor in governing the stability of the enzyme-substrate complex.The difference in the slope of the linear-regression lines seems to reflect the degree of relative hydrophobicity of the binding pockets in carboxypeptidase-Y and carboxypeptidase-A.
机译:研究了羧肽酶-Y和羧肽酶-A对二肽的酶解作用。在二肽的酶解过程中,Michaelis-Menten常数(K_m)与疏水性之间存在良好的线性关系(r = 0.997和0.999)。相关性表明,C末端氨基酸的疏水性是控制酶-底物复合物稳定性的主要因素。回归线似乎反映了羧肽酶-Y和羧肽酶-A中结合口袋的相对疏水程度。

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