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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ftdoajarticles:oai:doaj.org/article:bdf016d9e23e49eba9c8db7310530d47 2023-05-15T15:30:59+02:00 Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris 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 2022-12-01T00:00:00Z https://doi.org/10.1080/14756366.2022.2080818 https://doaj.org/article/bdf016d9e23e49eba9c8db7310530d47 EN eng Taylor & Francis Group https://www.tandfonline.com/doi/10.1080/14756366.2022.2080818 https://doaj.org/toc/1475-6366 https://doaj.org/toc/1475-6374 doi:10.1080/14756366.2022.2080818 1475-6374 1475-6366 https://doaj.org/article/bdf016d9e23e49eba9c8db7310530d47 Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 37, Iss 1, Pp 1577-1586 (2022) Carbonic anhydrase Gyrodactylus salaris kinetics anion inhibitors sulphamic acid Therapeutics. Pharmacology RM1-950 article 2022 ftdoajarticles https://doi.org/10.1080/14756366.2022.2080818 2022-12-30T23:53:38Z 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. Article in Journal/Newspaper Atlantic salmon Directory of Open Access Journals: DOAJ Articles Journal of Enzyme Inhibition and Medicinal Chemistry 37 1 1577 1586 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Carbonic anhydrase Gyrodactylus salaris kinetics anion inhibitors sulphamic acid Therapeutics. Pharmacology RM1-950 |
spellingShingle |
Carbonic anhydrase Gyrodactylus salaris kinetics anion inhibitors sulphamic acid Therapeutics. Pharmacology RM1-950 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 Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris |
topic_facet |
Carbonic anhydrase Gyrodactylus salaris kinetics anion inhibitors sulphamic acid Therapeutics. Pharmacology RM1-950 |
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. |
format |
Article in Journal/Newspaper |
author |
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 |
author_facet |
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 |
author_sort |
Ashok Aspatwar |
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 |
publisher |
Taylor & Francis Group |
publishDate |
2022 |
url |
https://doi.org/10.1080/14756366.2022.2080818 https://doaj.org/article/bdf016d9e23e49eba9c8db7310530d47 |
genre |
Atlantic salmon |
genre_facet |
Atlantic salmon |
op_source |
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 37, Iss 1, Pp 1577-1586 (2022) |
op_relation |
https://www.tandfonline.com/doi/10.1080/14756366.2022.2080818 https://doaj.org/toc/1475-6366 https://doaj.org/toc/1475-6374 doi:10.1080/14756366.2022.2080818 1475-6374 1475-6366 https://doaj.org/article/bdf016d9e23e49eba9c8db7310530d47 |
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_ |
1766361461843558400 |