Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris
A β-class carbonic anhydrase (CA, EC 4.2.1.1) 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−...
Published in: | Journal of Enzyme Inhibition and Medicinal Chemistry |
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2022
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Online Access: | https://trepo.tuni.fi/handle/10024/141798 https://doi.org/10.1080/14756366.2022.2080818 |
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ftunivtampere:oai:trepo.tuni.fi:10024/141798 2024-01-07T09:42:13+01:00 Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris Aspatwar, Ashok Barker, Harlan Aisala, Heidi Zueva, Ksenia Kuuslahti, Marianne Tolvanen, Martti Primmer, Craig R. Lumme, Jaakko Bonardi, Alessandro Tripathi, Amit Parkkila, Seppo Supuran, Claudiu T. Tampere University BioMediTech Clinical Medicine Department of Clinical Chemistry 2022 10 3512776 fulltext https://trepo.tuni.fi/handle/10024/141798 https://doi.org/10.1080/14756366.2022.2080818 en eng 1 37 1475-6366 ORCID: /0000-0001-7323-8536/work/131693685 https://trepo.tuni.fi/handle/10024/141798 URN:NBN:fi:tuni-202208196555 doi:10.1080/14756366.2022.2080818 cc by 4.0 openAccess 3111 Biomedicine article 2022 ftunivtampere https://doi.org/10.1080/14756366.2022.2080818 2023-12-14T00:08:24Z A β-class carbonic anhydrase (CA, EC 4.2.1.1) 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. Peer reviewed Article in Journal/Newspaper Atlantic salmon Tampere University: Trepo Journal of Enzyme Inhibition and Medicinal Chemistry 37 1 1577 1586 |
institution |
Open Polar |
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Tampere University: Trepo |
op_collection_id |
ftunivtampere |
language |
English |
topic |
3111 Biomedicine |
spellingShingle |
3111 Biomedicine Aspatwar, Ashok Barker, Harlan Aisala, Heidi Zueva, Ksenia Kuuslahti, Marianne Tolvanen, Martti Primmer, Craig R. Lumme, Jaakko Bonardi, Alessandro Tripathi, Amit Parkkila, Seppo Supuran, Claudiu T. Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris |
topic_facet |
3111 Biomedicine |
description |
A β-class carbonic anhydrase (CA, EC 4.2.1.1) 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. Peer reviewed |
author2 |
Tampere University BioMediTech Clinical Medicine Department of Clinical Chemistry |
format |
Article in Journal/Newspaper |
author |
Aspatwar, Ashok Barker, Harlan Aisala, Heidi Zueva, Ksenia Kuuslahti, Marianne Tolvanen, Martti Primmer, Craig R. Lumme, Jaakko Bonardi, Alessandro Tripathi, Amit Parkkila, Seppo Supuran, Claudiu T. |
author_facet |
Aspatwar, Ashok Barker, Harlan Aisala, Heidi Zueva, Ksenia Kuuslahti, Marianne Tolvanen, Martti Primmer, Craig R. Lumme, Jaakko Bonardi, Alessandro Tripathi, Amit Parkkila, Seppo Supuran, Claudiu T. |
author_sort |
Aspatwar, Ashok |
title |
Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris |
title_short |
Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris |
title_full |
Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris |
title_fullStr |
Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris |
title_full_unstemmed |
Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris |
title_sort |
cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the atlantic salmon parasite platyhelminth gyrodactylus salaris |
publishDate |
2022 |
url |
https://trepo.tuni.fi/handle/10024/141798 https://doi.org/10.1080/14756366.2022.2080818 |
genre |
Atlantic salmon |
genre_facet |
Atlantic salmon |
op_relation |
1 37 1475-6366 ORCID: /0000-0001-7323-8536/work/131693685 https://trepo.tuni.fi/handle/10024/141798 URN:NBN:fi:tuni-202208196555 doi:10.1080/14756366.2022.2080818 |
op_rights |
cc by 4.0 openAccess |
op_doi |
https://doi.org/10.1080/14756366.2022.2080818 |
container_title |
Journal of Enzyme Inhibition and Medicinal Chemistry |
container_volume |
37 |
container_issue |
1 |
container_start_page |
1577 |
op_container_end_page |
1586 |
_version_ |
1787423141701615616 |