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Cloning and characterization of a new cold-active lipase from a deep-sea sediment metagenome.从深海沉积物宏基因组中克隆并鉴定一种新型冷活性脂肪酶
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Engineering of Pseudomonas aeruginosa lipase by directed evolution for enhanced amidase activity: mechanistic implication for amide hydrolysis by serine hydrolases.通过定向进化工程改造铜绿假单胞菌脂肪酶以增强酰胺酶活性：丝氨酸水解酶催化酰胺水解的机制研究
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通过宏基因组学方法分离得到的一种真正的脂肪酶LipC12的结晶及初步晶体学分析

Crystallization and preliminary crystallographic analysis of LipC12, a true lipase isolated through a metagenomics approach.

作者信息

Martini V P, Glogauer A, Iulek J, Souza E M, Pedrosa F O, Krieger N

机构信息

Department of Chemistry, Federal University of Paraná, Curitiba-PR, Brazil.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt 2):175-7. doi: 10.1107/S1744309111051323. Epub 2012 Jan 26.

DOI:10.1107/S1744309111051323
PMID:22297992
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3274396/
Abstract

LipC12, a true lipase from family I.1 of bacterial lipases which was previously isolated through a metagenomics approach, contains 293 amino acids. Among lipases of known three-dimensional structure, it has a sequence identity of 47% to the lipase from Pseudomonas aeruginosa PAO1. Recombinant N-terminally His(6)-tagged LipC12 protein was expressed in Escherichia coli, purified in a homogenous form and crystallized in several conditions, with the best crystals being obtained using 2.0 M sodium formate and 0.1 M bis-tris propane pH 7.0. X-ray diffraction data were collected to 2.70 Å resolution. The crystals belonged to the tetragonal space group P4(1)22, with unit-cell parameters a = b = 58.62, c = 192.60 Å.

摘要

LipC12是一种来自细菌脂肪酶I.1家族的真正脂肪酶，此前通过宏基因组学方法分离得到，含有293个氨基酸。在已知三维结构的脂肪酶中，它与铜绿假单胞菌PAO1的脂肪酶序列同一性为47%。重组的N端带有His(6)标签的LipC12蛋白在大肠杆菌中表达，以均一形式纯化，并在多种条件下结晶，使用2.0 M甲酸钠和0.1 M双三羟甲基氨基甲烷pH 7.0获得了最佳晶体。X射线衍射数据收集至2.70 Å分辨率。晶体属于四方晶系空间群P4(1)22，晶胞参数a = b = 58.62，c = 192.60 Å。