N-溴代琥珀酰亚胺对青蟹（锯缘青蟹）碱性磷酸酶的抑制动力学
Kinetics of inhibition of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide.
作者信息
Chen Q X, Zhang W, Zheng W Z, Zhao H, Yan S X, Wang H R, Zhou H M
机构信息
Department of Biology, Xiamen University, China.
出版信息
J Protein Chem. 1996 May;15(4):345-50. doi: 10.1007/BF01886860.
The inactivation of alkaline phosphatase from green crab (Scylla serrata) by N-bromosuccinimide has been studied using the kinetic method of the substrate reaction during modification of enzyme activity previously described by Tsou [(1988), Adv. Enzymol. Related Areas Mol. Biol. 61, 381-436]. The results show that inactivation of the enzyme is a slow, reversible reaction. The microscopic rate constants for the reaction of the inactivator with free enzyme and the enzyme-substrate complex were determined. Comparison of these rate constants indicates that the presence of substrate offers marked protection of this enzyme against inactivation by N-bromosuccinimide. The above results suggest that the tryptophan residue is essential for activity and is situated at the active site of the enzyme.
采用邹[(1988年)，《酶学及相关领域分子生物学进展》61卷，381 - 436页]先前描述的在酶活性修饰过程中底物反应的动力学方法，研究了N - 溴代琥珀酰亚胺对青蟹（锯缘青蟹）碱性磷酸酶的失活作用。结果表明，该酶的失活是一个缓慢的、可逆的反应。测定了失活剂与游离酶及酶 - 底物复合物反应的微观速率常数。这些速率常数的比较表明，底物的存在对该酶具有显著的保护作用，使其免受N - 溴代琥珀酰亚胺的失活作用。上述结果表明，色氨酸残基对活性至关重要，且位于酶的活性部位。
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