title: Characterization of a novel exported esterase Rv3036c from Mycobacterium tuberculosis.
abstract: 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 (C2) 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.
authors.affiliation: Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 15000, PR China.
authors.forename: Liping
authors.initials: L
authors.lastname: Chen
authors.affiliation: Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 15000, PR China; School of Medicine, Tsinghua University, Beijing 100084, PR China; Fujian Agriculture and Forestry University, Fuzhou 350002, PR China.
authors.forename: Guanghui
authors.initials: G
authors.lastname: Dang
authors.affiliation: School of Medicine, Tsinghua University, Beijing 100084, PR China.
authors.forename: Xiaoxia
authors.initials: X
authors.lastname: Deng
authors.affiliation: Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 15000, PR China.
authors.forename: Jun
authors.initials: J
authors.lastname: Cao
authors.affiliation: Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 15000, PR China.
authors.forename: Shenye
authors.initials: S
authors.lastname: Yu
authors.affiliation: Fujian Agriculture and Forestry University, Fuzhou 350002, PR China.
authors.forename: Defeng
authors.initials: D
authors.lastname: Wu
authors.affiliation: School of Medicine, Tsinghua University, Beijing 100084, PR China. Electronic address: pangh@xtal.tsinghua.edu.cn.
authors.forename: Hai
authors.initials: H
authors.lastname: Pang
authors.affiliation: Division of Bacterial Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 15000, PR China. Electronic address: siguo_liu@hvri.ac.cn.
authors.forename: Siguo
authors.initials: S
authors.lastname: Liu
mesh_terms: D000595:Amino Acid Sequence; D004789:Enzyme Activation; D004926:Escherichia coli; D004950:Esterases / Q000096:biosynthesis / Q000302:isolation & purification*; D009169:Mycobacterium tuberculosis / Q000201:enzymology*; D009596:Nitrophenols / Q000378:metabolism; D021382:Protein Sorting Signals
chemical_list: D009596:Nitrophenols; D021382:Protein Sorting Signals; C008642:4-nitrophenyl acetate; D004950:Esterases
keywords: Exported esterase; Mycobacterium tuberculosis; rv3036c