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嗜酸 Alicyclobacillus 羧基酯酶 EST2 的结构与动力学概述:与 HSL 家族其他成员的比较。

Structural and kinetic overview of the carboxylesterase EST2 from alicyclobacillus acidocaldarius: a comparison with the other members of the HSL family.

作者信息

Mandrich Luigi, Merone Luigia, Manco Giuseppe

机构信息

Institute of Protein Biochemistry (IBP), National Research Council (CNR), Via Pietro Castellino 111, 80131, Naples, Italy.

出版信息

Protein Pept Lett. 2009;16(10):1189-200. doi: 10.2174/092986609789071261.

DOI:10.2174/092986609789071261
PMID:19508183
Abstract

Thermophilic and hyperthermophilic carboxylesterases (EC 3.1.1.1) are excellent model systems for studying structure function relationships as well as in vitro and in vivo evolution and possible biotechnological applications. In this paper we review the main aspect of one of most studied microbial representative of the hormone sensitive lipase family (HSL), namely carboxylesterase 2 (EST2) from Alicyclobacillus acidocaldarius.

摘要

嗜热和超嗜热羧酸酯酶(EC 3.1.1.1)是用于研究结构功能关系以及体外和体内进化及可能的生物技术应用的优秀模型系统。在本文中,我们综述了激素敏感脂肪酶家族(HSL)中研究最多的微生物代表之一,即嗜酸 Alicyclobacillus 酸热菌的羧酸酯酶2(EST2)的主要方面。

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Structural and kinetic overview of the carboxylesterase EST2 from alicyclobacillus acidocaldarius: a comparison with the other members of the HSL family.嗜酸 Alicyclobacillus 羧基酯酶 EST2 的结构与动力学概述:与 HSL 家族其他成员的比较。
Protein Pept Lett. 2009;16(10):1189-200. doi: 10.2174/092986609789071261.
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Computational analysis of carboxylesterase genes and proteins in non-pathogenic food bacterium Alicyclobacillus acidocaldarius: insights from proteogenomics.非致病食品细菌中羧酸酯酶基因和蛋白质的计算分析:来自蛋白质基因组学的见解。
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The first dipeptidyl peptidase III from a thermophile: Structural basis for thermal stability and reduced activity.来自嗜热菌的首个二肽基肽酶III:热稳定性和活性降低的结构基础。
PLoS One. 2018 Feb 8;13(2):e0192488. doi: 10.1371/journal.pone.0192488. eCollection 2018.
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