一种小型嵌合双功能单体蛋白：日本磁带溶菌酶。
A small chimerically bifunctional monomeric protein: Tapes japonica lysozyme.
作者信息
Takeshita K, Hashimoto Y, Ueda T, Imoto T
机构信息
Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka, 812-8582, Japan.
出版信息
Cell Mol Life Sci. 2003 Sep;60(9):1944-51. doi: 10.1007/s00018-003-3082-z.
The lysozyme of the marine bilave Tapes japonica (13.8 kDa) is a novel protein. The protein has 46% homology with the destabilase from medicinal leech that has isopeptidase activity. Based on these data, we confirmed hydrolysis activity of T. japonica lysozyme against three substrates: L-gamma-Glu-pNA, D-gamma-Glu-pNA, and epsilon-(gamma-Glu)-L-Lys. The optimal pH of chitinase and isopeptidase activity was 5.0 and 7.0, respectively. The isopeptidase activity was inhibited with serine protease inhibitor, but the lytic and chitinase activities were not. Moreover, only isopeptidase activity is decreased by lyophilization, but lytic and chitinase activities were not. We conclude that T. japonica lysozyme expresses isopeptidase and chitinase activity at different active sites.
海洋双壳贝类日本镜蛤（13.8 kDa）的溶菌酶是一种新型蛋白质。该蛋白质与具有异肽酶活性的药用蚂蟥去稳定酶有46%的同源性。基于这些数据，我们证实了日本镜蛤溶菌酶对三种底物的水解活性：L-γ-谷氨酰-对硝基苯胺、D-γ-谷氨酰-对硝基苯胺和ε-（γ-谷氨酰）-L-赖氨酸。几丁质酶和异肽酶活性的最适pH分别为5.0和7.0。异肽酶活性被丝氨酸蛋白酶抑制剂抑制，但溶菌和几丁质酶活性不受影响。此外，只有异肽酶活性在冻干后降低，而溶菌和几丁质酶活性不受影响。我们得出结论，日本镜蛤溶菌酶在不同的活性位点表达异肽酶和几丁质酶活性。
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