| 化学修饰对青霉素G酰化酶活性的影响 |
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| 引用本文： | 陈红,颜茂恭,张其玖.化学修饰对青霉素G酰化酶活性的影响[J].中国生物化学与分子生物学报,1991,7(6):667-670. |
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| 作者姓名： | 陈红 颜茂恭 张其玖 |
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| 作者单位： | 中国科学院生物物理研究所，中国科学院生物物理研究所，中国科学院生物物理研究所 北京 100080，北京 100080，北京 100080 |
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| 摘 要： | 为进一步阐明大肠杆菌AE 109青霉素G酰化酶(PA,E.C.3.5.1.11)的结构与功能关系,研究了数种修饰剂对酶活性的影响;同时测定了四种作用物存在下对各修饰剂修饰酶的影响。结果表明Ser残基处于酶的活性部位,Met残基可能处于与底物结合的部位,His和Cys残基与酶的活性无关。
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| 关 键 词： | 青霉素G酰化酶 化学修饰 酶活性 |
| 收稿时间： | 1991-12-20 |
Effect of Chemical Modification on the Enzymatic Activity of Penicillin G Acylase |
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| Chen,Hong Yan,Mao-gong Zhang,Qi-jiu.Effect of Chemical Modification on the Enzymatic Activity of Penicillin G Acylase[J].Chinese Journal of Biochemistry and Molecular Biology,1991,7(6):667-670. |
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| Authors: | Chen Hong Yan Mao-gong Zhang Qi-jiu |
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| Institution: | (Institute of Biophysics, Academia Sinica, Beijing 100080 |
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| Abstract: | In order to elucidate the structure-function relationship of Penicillin G acylase (PA, E.G.3.5.1.11) from E.coli AE 109, the effect of chemical modification on the enzymztic activity has been studied. The results showed that serine residue wes in the active site, methionine residue was possibly in the substrate binding site. Histidine and cysteine residues were not related to the enzymatic activity. |
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| Keywords: | Penicillin G acylase Chemical modification Enzymatic activity |
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