Expression and functional analysis of a predicted atsg arylsulphatase identified from mycobacterium tuberculosis genomic data

Md Murad Hossain, Yutaka Kawarabayasi, Makoto Kimura, Yoshimitsu Kakuta

研究成果: ジャーナルへの寄稿記事

6 引用 (Scopus)

抄録

Sulphatase family enzymes hydrolyse the sulphate ester, found on the pathogens cell surface and playing an important role for host-pathogen interaction. The AtsG, homologue of arylsulphatase, predicted in the Mycobacterium tuberculosis genomic data, was successfully expressed in Escherichia coli. The recombinant AtsG protein exhibited hydrolysis of para-nitrophenyl sulphate and para-nitrocatechol sulphate, and binding affinity to the heparin-sepharose resin. This is the first report of molecular evidence for an arylsulphatase activity of the AtsG protein. The maximum activity was detected at pH 8.0 and 37°C. As EDTA completely inhibited this activity, a divalent cation was required for the activity.

元の言語英語
ページ(範囲)767-769
ページ数3
ジャーナルJournal of biochemistry
146
発行部数6
DOI
出版物ステータス出版済み - 12 1 2009

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Arylsulfatases
Functional analysis
Pathogens
Mycobacterium tuberculosis
Sulfatases
Host-Pathogen Interactions
Divalent Cations
Recombinant Proteins
Edetic Acid
Escherichia coli
Sulfates
Hydrolysis
Esters
Resins
Enzymes
Proteins
4-nitrophenyl sulfate
heparin-sepharose
4-nitrocatechol sulfate

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

これを引用

Expression and functional analysis of a predicted atsg arylsulphatase identified from mycobacterium tuberculosis genomic data. / Hossain, Md Murad; Kawarabayasi, Yutaka; Kimura, Makoto; Kakuta, Yoshimitsu.

:: Journal of biochemistry, 巻 146, 番号 6, 01.12.2009, p. 767-769.

研究成果: ジャーナルへの寄稿記事

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