Journal
JOURNAL OF BIOCHEMISTRY
Volume 146, Issue 6, Pages 767-769Publisher
OXFORD UNIV PRESS
DOI: 10.1093/jb/mvp141
Keywords
arylsulphatase; heparin-sepharose resin binding affinity; Mycobacterium tuberculosis; para-nitrocatechol sulphate; para-nitrophenyl sulphate
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Funding
- Ministry of Education, Culture, Sports, Science and Technology, Japan
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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 degrees C. As EDTA completely inhibited this activity, a divalent cation was required for the activity.
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