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Comprehensive kinetic and substrate specificity analysis of an arylsulfatase from Helix pomatia using mass spectrometry
Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Chemical Biology for Biomarker Discovery.ORCID iD: 0000-0003-2125-4184
Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Chemical Biology for Biomarker Discovery.ORCID iD: 0000-0002-3059-9013
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry. Uppsala University, Science for Life Laboratory, SciLifeLab.
Uppsala University, Science for Life Laboratory, SciLifeLab. Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Medicinal Chemistry, Chemical Biology for Biomarker Discovery.
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2019 (English)In: Bioorganic & Medicinal Chemistry, ISSN 0968-0896, E-ISSN 1464-3391, Vol. 27, no 6, p. 955-962Article in journal (Refereed) Published
Abstract [en]

Sulfatases hydrolyze sulfated metabolites to their corresponding alcohols and are present in all domains of life. These enzymes have found major application in metabolic investigation of drugs, doping control analysis and recently in metabolomics. Interest in sulfatases has increased due to a link between metabolic processes involving sulfated metabolites and pathophysiological conditions in humans. Herein, we present the first comprehensive substrate specificity and kinetic analysis of the most commonly used aryl sulfatases extracted from the snail Helix pomatia. In the past, this enzyme has been used in the form of a crude mixture of enzymes, however, recently we have purified this sulfatase for a new application in metabolomics-driven discovery of sulfated metabolites. To evaluate the substrate specificity of this promiscuous sulfatase, we have synthesized a series of new sulfated metabolites of diverse structure and employed a mass spectrometric assay for kinetic substrate hydrolysis evaluation. Our analysis of the purified enzyme revealed that the sulfatase has a strong preference for metabolites with a bi- or tricyclic aromatic scaffold and to a lesser extent for monocyclic aromatic phenols. This metabolite library and mass spectrometric method can be applied for the characterization of other sulfatases from humans and gut microbiota to investigate their involvement in disease development.

Place, publisher, year, edition, pages
2019. Vol. 27, no 6, p. 955-962
Keywords [en]
Arylsulfatase, Helix pomatia, Substrate specificity, Xenobiotics, Phase II
National Category
Medicinal Chemistry Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-381821DOI: 10.1016/j.bmc.2019.01.031ISI: 000462478700004PubMedID: 30738652OAI: oai:DiVA.org:uu-381821DiVA, id: diva2:1306651
Funder
Swedish Research Council, 2016-04423Carl Tryggers foundation , 2016:155Science for Life Laboratory - a national resource center for high-throughput molecular bioscienceAvailable from: 2019-04-24 Created: 2019-04-24 Last updated: 2019-04-24Bibliographically approved

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Correia, Mário S. P.Ballet, CarolineConway, Louis P.Globisch, Daniel

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