Characterization of a novel exported esterase Rv3036c from Mycobacterium tuberculosis

文献类型： 外文期刊

第一作者： Chen, Liping

作者： Chen, Liping;Dang, Guanghui;Cao, Jun;Yu, Shenye;Liu, Siguo;Dang, Guanghui;Deng, Xiaoxia;Pang, Hai;Dang, Guanghui;Wu, Defeng

作者机构：

关键词： Mycobacterium tuberculosis;Exported esterase;rv3036c

期刊名称：PROTEIN EXPRESSION AND PURIFICATION （ 影响因子：1.65； 五年影响因子：1.548 ）

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收录情况： SCI

摘要： 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.

分类号： Q51

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