STAPHYLOCOCCAL L-ASPARAGINASE - ENZYME-KINETICS

被引：0
|
作者：
SOBIS, M
MIKUCKI, J
机构：
来源：
ACTA MICROBIOLOGICA POLONICA | 1991年 / 40卷 / 3-4期
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中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
The ph optimum of purified staphylococcal L-asparaginase (EC 3.5.1.1) was found to be between 8.6 and 8.8. The temperature optimum was 30-degrees-32-degrees-C and the highest reaction rate occurred at 30-degrees-C. The K(M) of the enzyme calculated from Lineweaver-Burk plot was 3.71 x 10(-2)M. Besides L-asparaginase, the substrate specificity of enzyme was restricted to N-alpha-acetyl-L-asparagine. D-asparagine, L-asparatic acid and D-glumtic acid were competitive inhibitors. Hg2+ and Cu2+ cations strongly inhibited the enzyme while Na+ and K+ cations strongly stimulated activity. Two SH-groups could be detected after enzyme denaturation with guanidine.
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页码：143 / 152
页数：10
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