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通过改善内部氢键作用提高嗜热脂肪芽孢杆菌中性蛋白酶的热稳定性。

Increasing the thermostability of the neutral proteinase of Bacillus stearothermophilus by improvement of internal hydrogen-bonding.

作者信息

Eijsink V G, Vriend G, Van der Zee J R, Van den Burg B, Venema G

机构信息

Department of Molecular Genetics, University of Groningen, Haren, The Netherlands.

出版信息

Biochem J. 1992 Jul 15;285 ( Pt 2)(Pt 2):625-8. doi: 10.1042/bj2850625.

Abstract

In an attempt to increase the thermostability of the neutral proteinase of Bacillus stearothermophilus the buried Ala-170 was replaced by serine. Molecular-dynamics simulations showed that Ser-170 stabilizes the enzyme by formation of an internal hydrogen bond. In addition, the hydroxy group of Ser-170 could contribute to stability by filling an internal cavity. After the introduction of the mutation, using site-directed-mutagenesis techniques, an increase in stability of 0.7 +/- 0.1 degrees C was obtained.

摘要

为提高嗜热脂肪芽孢杆菌中性蛋白酶的热稳定性,将埋藏的丙氨酸-170替换为丝氨酸。分子动力学模拟表明,丝氨酸-170通过形成分子内氢键使酶稳定。此外,丝氨酸-170的羟基可通过填充内部空腔来提高稳定性。利用定点诱变技术引入突变后,稳定性提高了0.7±0.1摄氏度。

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本文引用的文献

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Hydrogen bonding in globular proteins.球状蛋白质中的氢键。
Prog Biophys Mol Biol. 1984;44(2):97-179. doi: 10.1016/0079-6107(84)90007-5.
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Neutral proteases of the genus Bacillus.
Biochem Biophys Res Commun. 1969 Jul 23;36(2):257-65. doi: 10.1016/0006-291x(69)90323-4.
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Energetics of protein structure and folding.蛋白质结构与折叠的能量学
Biopolymers. 1985 Jan;24(1):167-82. doi: 10.1002/bip.360240114.

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