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

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

Research output: Contribution to journalArticlepeer-review

7 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)767-769
Number of pages3
JournalJournal of biochemistry
Volume146
Issue number6
DOIs
Publication statusPublished - Dec 1 2009

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

Fingerprint Dive into the research topics of 'Expression and functional analysis of a predicted atsg arylsulphatase identified from mycobacterium tuberculosis genomic data'. Together they form a unique fingerprint.

Cite this