Characterization of a novel exported esterase Rv3036c from Mycobacterium tuberculosis
Characterization of a novel exported esterase Rv3036c from Mycobacterium tuberculosis
复制标题
结核分枝杆菌新型输出酯酶 Rv3036c 的表征
DOI：
10.1016/j.pep.2014.09.003
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发表时间：
2014-12-01
影响因子：
1.6
通讯作者：
Liu, Siguo
中科院分区：
文献类型：
--
作者：
Chen, Liping;Dang, Guanghui;Liu, Siguo
Mycobacterium tuberculosis possesses an unusually high number of genes involved in the metabolism of lipids. Driven by a newly described esterase motif SXXK in the amino acid sequence and a predicted signal peptide, the gene rv3036c from M. tuberculosis was cloned and characterized biochemically. Rv3036c efficiently hydrolyzes soluble p-nitrophenyl esters but not emulsified lipid. The highest activity of this enzyme was observed when p-nitrophenyl acetate (C-2) was used as the substrate. Based on the activities, Rv3036c was classified as a nonlipolytic hydrolase. The results of immunoreactivity studies on the subcellular mycobacterial fractions suggested that the enzyme was present in the cell wall and cell membrane in mycobacteria. In summary, Rv3036c was characterized as a novel cell wall-anchored esterase from M. tuberculosis. (C) 2014 Published by Elsevier Inc.
