人组织蛋白酶B。底物N-苄氧羰基-L-精氨酰-L-精氨酸2-萘酰胺在亮抑酶肽抑制作用研究中的应用。
Human cathepsin B. Application of the substrate N-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide to a study of the inhibition by leupeptin.
作者信息
Knight C G
出版信息
Biochem J. 1980 Sep 1;189(3):447-53. doi: 10.1042/bj1890447.
Abstract
- The kinetic parameters Kcat. and Km were determined for the hydrolysis of some arginine naphthylamides by human cathepsin B. 2. A new and efficient synthesis of Z-Arg-Arg-NNap (benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide) was developed. 3. Z-Arg-Arg-NNap was a specific and sensitive substrate for cathepsin B, and was used for kinetic studies. 4. Values of kcat. were maximal in the pH range 5.4--6.2, and depended on a single ionizing group of pKa 4.4. 5. Leupeptin was a purely competitive inhibitor of human cathepsin B. 6. The effect of pH on the apparent inhibitor constant, Ki (app.), was determined. Ki (app.) was pH-independent in the range pH 4.3--6.0, with the mean value 7 x 10(-9) M.
摘要
- 测定了人组织蛋白酶B水解某些精氨酸萘酰胺的动力学参数Kcat.和Km。2. 开发了一种新的、高效的Z-Arg-Arg-NNap（苄氧羰基-L-精氨酰-L-精氨酸2-萘酰胺）合成方法。3. Z-Arg-Arg-NNap是组织蛋白酶B的特异性敏感底物，用于动力学研究。4. kcat.值在pH 5.4 - 6.2范围内最大，且取决于pKa为4.4的单一电离基团。5. 亮抑酶肽是人类组织蛋白酶B的纯竞争性抑制剂。6. 测定了pH对表观抑制剂常数Ki（app.）的影响。在pH 4.3 - 6.0范围内，Ki（app.）与pH无关，平均值为7×10⁻⁹ M。
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本文引用的文献
1
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J Org Chem. 1965 Jun;30:1781-5. doi: 10.1021/jo01017a017.
2
Statistical estimations in enzyme kinetics.酶动力学中的统计估计
Biochem J. 1961 Aug;80(2):324-32. doi: 10.1042/bj0800324.
3
The determination of enzyme inhibitor constants.酶抑制剂常数的测定
Biochem J. 1953 Aug;55(1):170-1. doi: 10.1042/bj0550170.
4
The kinetics of the papain-catalyzed hydrolysis of esters of carbobenzoxyglycine. Evidence for an acyl-enzyme intermediate.对甲苯磺酰甘氨酸酯的木瓜蛋白酶催化水解动力学。酰基酶中间体的证据。
Biochemistry. 1966 Feb;5(2):783-91. doi: 10.1021/bi00866a053.
5
The topographical differences in the active site region of alpha-chymotrypsin, subtilisin Novo, and subtilisin Carlsberg. Mapping the aromatic binding site by inhibitors (virtual substrates).α-胰凝乳蛋白酶、嗜热栖热菌蛋白酶和枯草杆菌蛋白酶卡尔伯格活性位点区域的拓扑差异。通过抑制剂（虚拟底物）绘制芳香族结合位点。
Biochemistry. 1974 Jan 15;13(2):266-77. doi: 10.1021/bi00699a006.
6
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