α-胰凝乳蛋白酶的特异性和立体特异性
Specificity and stereospecificity of alpha-chymotrypsin.
作者信息
Ingles D W, Knowles J R
出版信息
Biochem J. 1967 Aug;104(2):369-77. doi: 10.1042/bj1040369.
Abstract
- The optically pure p-nitrophenyl esters of the d and l enantiomers of N-acetyl-tryptophan, N-acetylphenylalanine and N-acetyl-leucine, and the p-nitrophenyl ester of N-acetylglycine, have been prepared. 2. These materials are all substrates of alpha-chymotrypsin, and the rates of deacylation of the corresponding acyl-alpha-chymotrypsins have been determined. 3. As the size of the amino acid side chain increases, the l series deacylate progressively faster than the N-acetylglycyl-enzyme, and the d series progressively more slowly. 4. The results are interpreted in terms of a three-locus model of the enzyme's active site, which accounts for the interrelationship between substrate specificity and stereospecificity observed. 5. The concepts of negative specificity and of specificity saturation are introduced.
摘要
- 已制备出N - 乙酰色氨酸、N - 乙酰苯丙氨酸和N - 乙酰亮氨酸的d型和l型对映体的光学纯对硝基苯酯，以及N - 乙酰甘氨酸的对硝基苯酯。2. 这些物质均为α - 胰凝乳蛋白酶的底物，并且已测定了相应的酰基 - α - 胰凝乳蛋白酶的脱酰化速率。3. 随着氨基酸侧链尺寸的增加，l型系列的脱酰化速度比N - 乙酰甘氨酰 - 酶逐渐加快，而d型系列则逐渐减慢。4. 根据酶活性位点的三位点模型对结果进行了解释，该模型解释了所观察到的底物特异性和立体特异性之间的相互关系。5. 引入了负特异性和特异性饱和的概念。
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