苯乙二醛对锯缘青蟹碱性磷酸酶的抑制动力学
Kinetics of inhibition of green crab (Scylla serrata) alkaline phosphatase by phenylglyoxal.
作者信息
Xie W Z, Wang H R, Chen Q X, Zhou H M
机构信息
Department of Biological Science and Biotechnology, Tsinghua University, Beijing, P.R. China.
出版信息
Biochem Mol Biol Int. 1996 Nov;40(5):981-91. doi: 10.1080/15216549600201613.
The kinetics method of the substrate reaction during modification of enzyme activity previously described by Tsou (Adv. Enzymol. Related. Areas Mol. Biol., 1988, 61, 381-436) has been applied to study the kinetics of the course of inactivation of green crab alkaline phosphatase by phenylglyoxal. The obtained results shows that the inactivation of the enzyme by phenylglyoxal is a slow reversible reaction. The microscopic rate constants for the reaction of the inhibitor with the enzyme were determined. The presence of substrate offers marked protection of this enzyme against inactivation by phenylglyoxal. The above results suggest that the arginine residue is essential for activity and is situated at the active site of the enzyme.
邹（《酶学进展及相关分子生物学领域》，1988年，61卷，381 - 436页）先前描述的酶活性修饰过程中底物反应的动力学方法，已被用于研究苯乙二醛使青蟹碱性磷酸酶失活过程的动力学。所得结果表明，苯乙二醛使该酶失活是一个缓慢的可逆反应。测定了抑制剂与酶反应的微观速率常数。底物的存在对该酶有显著的保护作用，使其免受苯乙二醛的失活作用。上述结果表明，精氨酸残基对酶活性至关重要，且位于酶的活性位点。
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