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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural and functional analyses of a bacterial homologue of hormone-sensitive lipase from a metagenomic library
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Structural and functional analyses of a bacterial homologue of hormone-sensitive lipase from a metagenomic library

机译：细菌的结构和功能分析同系物的荷尔蒙脂肪酶宏基因组

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摘要

Intracellular mobilization of fatty acids from triacylglycerols in mammalian adipose tissues proceeds through a series of lipolytic reactions. Among the enzymes involved, hormone-sensitive lipase (HSL) is noteworthy for its central role in energy homeostasis and the pathogenic role played by its dysregulation. By virtue of its broad substrate specificity, HSL may also serve as an industrial biocatalyst. In a previous report, Est25, a bacterial homologue of HSL, was identified from a metagenomic library by functional screening. Here, the crystal structure of Est25 is reported at 1.49? resolution; it exhibits an /β-hydrolase fold consisting of a central β-sheet enclosed by -helices on both sides. The structural features of the cap domain, the substrate-binding pocket and the dimeric interface of Est25, together with biochemical and biophysical studies including native PAGE, mass spectrometry, dynamic light scattering, gel filtration and enzyme assays, could provide a basis for understanding the properties and regulation of hormone-sensitive lipase (HSL). The increased stability of cross-linked Est25 aggregates (CLEA-Est25) and their potential for extensive reuse support the application of this preparation as a biocatalyst in biotransformation processes.
机译：细胞内脂肪酸动员甘油三酯在哺乳动物脂肪组织通过一系列的分解脂肪的反应。所涉及的酶,荷尔蒙脂肪酶(奥软)是最引人注意的中心角色在能源体内平衡和致病作用由它的失调。广泛的底物特异性,高速逻辑也可能服务作为一个工业生物催化剂。报告,Est25,奥软的细菌同系物确定从宏基因组功能检查。在1.49 Est25的报道吗?展品an /β水解酶折叠组成的中央β片包围螺旋线上两侧。substrate-binding口袋里和二聚的接口Est25,生化和在一起生物物理的研究包括本地页面,质量光谱法、动态光散射、凝胶过滤和酶化验,可以提供理解属性和依据调节荷尔蒙脂肪酶(高速逻辑)。增加交联Est25的稳定总量(CLEA-Est25)和他们的潜力广泛支持的应用程序重用准备作为生物催化剂在生物转化流程。

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