肽基氯甲烷对脯氨酰内肽酶的失活作用。失活动力学及修饰位点的鉴定。
Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification.
作者信息
Stone S R, Rennex D, Wikstrom P, Shaw E, Hofsteenge J
机构信息
Friedrich Miescher-Institut, Basel, Switzerland.
出版信息
Biochem J. 1991 Jun 15;276 ( Pt 3)(Pt 3):837-40. doi: 10.1042/bj2760837.
Abstract
The kinetics of inactivation of prolyl endopeptidase by acetyl-Ala-Ala-Pro-CH2Cl were studied by progress-curve methods in the presence of substrate. The kinetic mechanism was found to involve the formation of an initial complex between the enzyme and the chloromethane followed by an inactivation step. The substrate was shown to compete for the formation of the initial complex, indicating that binding at the active site was a prerequisite for inactivation. After reaction of the enzyme with [3H]acetyl-Ala-Ala-Pro-CH2Cl, it was possible to isolate five labelled peptides. Four of these peptides contained a cysteine residue as the site of modification, whereas the fifth peptide contained no cysteine and a histidine residue was identified as the site of modification. This residue (His-680) probably represents the active-site histidine of prolyl endopeptidase.
摘要
在有底物存在的情况下，通过进程曲线法研究了乙酰 - 丙氨酸 - 丙氨酸 - 脯氨酸 - 二氯甲烷对脯氨酰内肽酶的失活动力学。发现动力学机制涉及酶与氯甲烷之间形成初始复合物，随后是失活步骤。结果表明底物竞争初始复合物的形成，这表明在活性位点的结合是失活的先决条件。酶与[³H]乙酰 - 丙氨酸 - 丙氨酸 - 脯氨酸 - 二氯甲烷反应后，可以分离出五种标记肽。其中四种肽含有半胱氨酸残基作为修饰位点，而第五种肽不含半胱氨酸，并且鉴定出组氨酸残基为修饰位点。该残基（His - 680）可能代表脯氨酰内肽酶的活性位点组氨酸。
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