单氨基酸置换对固定化酶热稳定性的提高是起促进作用还是起阻碍作用？
Does single-amino-acid replacement work in favor of or against improvement of the thermostability of immobilized enzyme?
作者信息
Koizumi J, Zhang M, Imanaka T, Aiba S
机构信息
Department of Applied Biology, Shimane University, Japan.
出版信息
Appl Environ Microbiol. 1990 Nov;56(11):3612-4. doi: 10.1128/aem.56.11.3612-3614.1990.
Abstract
Thermostabilities of kanamycin nucleotidyltransferase and of its mutants that became thermostable, in the free state, because of single-amino-acid replacements were studied after immobilization of the enzymes on cyanogen bromide-activated Sephadex G-200 particles. Lys in place of Gln at position 102 decreased the thermostability of the immobilized enzyme, whereas replacement with other amino acids enhanced it.
摘要
在将卡那霉素核苷酸转移酶及其因单氨基酸替换而在游离状态下变得热稳定的突变体固定在溴化氰活化的葡聚糖凝胶G - 200颗粒上之后，研究了它们的热稳定性。102位的谷氨酰胺被赖氨酸取代降低了固定化酶的热稳定性，而被其他氨基酸取代则提高了热稳定性。
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本文引用的文献
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Purification and characterization of a kanamycin nucleotidyltransferase from plasmid pUB110-carrying cells of Bacillus subtilis.来自携带质粒pUB110的枯草芽孢杆菌细胞的卡那霉素核苷酸转移酶的纯化及特性分析
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8
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