| 青霉素G酰化酶α亚基Ser177的突变对酶活性的影响 |
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| 引用本文： | 王敏,费俭,郭礼和,张其玖. 青霉素G酰化酶α亚基Ser177的突变对酶活性的影响[J]. 分子细胞生物学报, 1991, 0(1) |
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| 作者姓名： | 王敏 费俭 郭礼和 张其玖 |
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| 作者单位： | 中国科学院上海细胞生物学研究所(王敏，费俭，郭礼和)，中国科学院生物物理研究所(张其玖) |
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| 摘 要： | 用盒式突变和定点突变对大肠杆菌青霉素G酰化酶α亚基177位ser进行了突变研究,结果发现所挑选的突变体均无酶的活力,这一结果可能可以用来解释Ser 177附近肽段和一些青霉素结合蛋白青霉素结合区在一级结构上保持同源性的原因。
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| 关 键 词： | 青霉素G酰化酶基因 α亚基 盒式突变 点突变 |
EFFECT OF MUTAGENESIS AT Ser 177 RESIDURE IN PENICILLIN G ACYLASE ON ACTIVITY OF THE ENZYME |
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| Wang Min Fei Jian Guo Li-he. EFFECT OF MUTAGENESIS AT Ser 177 RESIDURE IN PENICILLIN G ACYLASE ON ACTIVITY OF THE ENZYME[J]. Journal of Molecular Cell Biology, 1991, 0(1) |
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| Authors: | Wang Min Fei Jian Guo Li-he |
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| Abstract: | The technique of cassette and site-specific mutagenesis were used to study the role of residue No. 177 in penicillin G acylase (PGA, EC3.5.1.11). Set is conserved at residue No. 177 in all penicillin binding proteins. We got a series of mutants in which the amino acid at residue No. 177 was replaced by other amino acids through the site-specific and cassette mutagenesis, and we characterized the mutants by colony hybridization, NIPAB paper test and DNA sequence analysis. These mutants all show no activity of enzyme, even if the Ser residue was replaced by Thr, Gly and Ala respectively. The results show that Ser residue may be essential for substractbinding or catalysis of PGA. |
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| Keywords: | Penicillin G Acylase. Site-specific mutagenesis. Cassette mutagenesi. Subunit. |
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