Preparation of chromophoric substrates for the glutamoyl specific staphylococcal protease.
Preparation of chromophoric substrates for the glutamoyl specific staphylococcal protease.
复制标题
谷氨酰特异性葡萄球菌蛋白酶发色底物的制备。
DOI：
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发表时间：
2009
期刊：
影响因子：
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通讯作者：
J. Houmard
中科院分区：
文献类型：
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作者：
J. Houmard
描述了允许准确测定葡萄球菌蛋白酶活性的发色底物的合成。制备了BOC-L-Glu-OPh、BOC-L-Phe-L-Glu-OPh、BOC-L-Ala-L-Glu-OPh、BOC-L-Ser-L-Glu-OPh和Z-L-Glu-pNA。葡萄球菌蛋白酶催化水解这些底物的动力学参数进行了比较。在每种情况下，与BOC-L-Glu-OPh或Z-L-Glu-OPh相比，二肽酯底物导致较低的催化效率（kcat/Km比），主要是因为Km值增加。与其它丝氨酸蛋白酶一样，葡萄球菌蛋白酶表现出高的酯酶与肽酶活性比，Z-L-Glu-OPh的kcat/Km比是Z-L-Glu-pNA的2.6 × 10（5）倍。
The synthesis of chromophoric substrates allowing an accurate determination of the staphylococcal protease activity is described. BOC-L-Glu-OPh, BOC-L-Phe-L-Glu-OPh, BOC-L-Ala-L-Glu-OPh, BOC-L-Ser-L-Glu-OPh and Z-L-Glu-pNA were prepared. Kinetic parameters of the staphyloccal protease-catalysed hydrolyses of these substrates are compared. In every case the dipeptide ester substrates lead to a lower catalytic efficiency (kcat/Km ratio), compared with either BOC-L-Glu-OPh or Z-L-Glu-OPh, mainly because of an increase in the Km value. Like other serine proteinases, the staphylococcal protease exhibits a high ratio of eeterase to peptidase activity, the kcat/Km ratio being 2.6 X 10(5)-fold higher with the Z-L-Glu-OPh than with the Z-L-Glu-pNA.