University of Oulu

Ashok Aspatwar, Harlan Barker, Heidi Aisala, Ksenia Zueva, Marianne Kuuslahti, Martti Tolvanen, Craig R. Primmer, Jaakko Lumme, Alessandro Bonardi, Amit Tripathi, Seppo Parkkila & Claudiu T. Supuran (2022) Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris, Journal of Enzyme Inhibition and Medicinal Chemistry, 37:1, 1577-1586, DOI: 10.1080/14756366.2022.2080818

Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris

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Author: Aspatwar, Ashok1; Barker, Harlan1; Aisala, Heidi2;
Organizations: 1Faculty of Medicine and Health Technology, Tampere University, Tampere, Finland
2Ecology and Genetics, University of Oulu, Oulu, Finland
3Department of Biology, University of Turku, Turku, Finland
4Department of Computing, University of Turku, Turku, Finland
5Organismal and Evolutionary Biology Research Programme, University of Helsinki, Helsinki, Finland
6Institute of Biotechnology, Helsinki Institute of Life Science, University of Helsinki, Helsinki, Finland
7Department of Neuroscience, Psychology, Drug Research and Child’s Health, Section of Pharmaceutical and Nutraceutical Sciences, University of Florence, Sesto Fiorentino, Italy
8Department of Zoology, University of Lucknow, Lucknow, India
9Fimlab Ltd, Tampere University Hospital, Tampere, Finland
Format: article
Version: published version
Access: open
Online Access: PDF Full Text (PDF, 3.3 MB)
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Language: English
Published: Informa, 2022
Publish Date: 2022-06-02


A β-class carbonic anhydrase (CA, EC was cloned from the genome of the Monogenean platyhelminth Gyrodactylus salaris, a parasite of Atlantic salmon. The new enzyme, GsaCAβ has a significant catalytic activity for the physiological reaction, CO₂ + H₂O ⇋ HCO₃⁻ + H⁺ with a kcat of 1.1 × 10⁵ s⁻¹ and a kcat/Km of 7.58 × 10⁶ M⁻¹ × s⁻¹. This activity was inhibited by acetazolamide (KI of 0.46 µM), a sulphonamide in clinical use, as well as by selected inorganic anions and small molecules. Most tested anions inhibited GsaCAβ at millimolar concentrations, but sulfamide (KI of 81 µM), N,N-diethyldithiocarbamate (KI of 67 µM) and sulphamic acid (KI of 6.2 µM) showed a rather efficient inhibitory action. There are currently very few non-toxic agents effective in combating this parasite. GsaCAβ is subsequently proposed as a new drug target for which effective inhibitors can be designed.

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Series: Journal of enzyme inhibition and medicinal chemistry
ISSN: 1475-6366
ISSN-E: 1475-6374
ISSN-L: 1475-6366
Volume: 37
Issue: 1
Pages: 1577 - 1586
DOI: 10.1080/14756366.2022.2080818
Type of Publication: A1 Journal article – refereed
Field of Science: 1181 Ecology, evolutionary biology
Funding: This research was financed by the Italian Ministry for Education and Science (MIUR), grant PRIN: rot. [2017XYBP2R]; Ente Cassa di Risparmio di Firenze (ECRF), grant [CRF2020.1395] (to CTS); Academy of Finland (to SP); Jane & Aatos Erkko Foundation (to SP); Finnish Cultural Foundation (to AA); and Tampere Tuberculosis Foundation (to AA).
Copyright information: © 2022 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.