کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2020437 1542337 2014 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Characterization of a novel exported esterase Rv3036c from Mycobacterium tuberculosis
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Characterization of a novel exported esterase Rv3036c from Mycobacterium tuberculosis
چکیده انگلیسی


• The esterase motif SXXK was identified in Rv3036c from M. tuberculosis.
• A highly pure soluble recombinant Rv3036c was obtained.
• Rv3036c showed hydrolase activity for water-soluble esters.
• Rv3036c was present at the surface of mycobacteria.

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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Protein Expression and Purification - Volume 104, December 2014, Pages 50–56
نویسندگان
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