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, CO 2 + H 2 O ⇋ HCO 3 − + H + with a k cat of 1.1 ×...
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| Published in: | Journal of enzyme inhibition and medicinal chemistry Vol. 37; no. 1; pp. 1577 - 1586 |
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| Main Authors: | , , , , , , , , , , , |
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| Language: | English |
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01-12-2022
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| Abstract | 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, CO
2
+ H
2
O ⇋ HCO
3
−
+ H
+
with a k
cat
of 1.1 × 10
5
s
−1
and a k
cat
/K
m
of 7.58 × 10
6
M
−1
× s
−1
. This activity was inhibited by acetazolamide (K
I
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 (K
I
of 81 µM), N,N-diethyldithiocarbamate (K
I
of 67 µM) and sulphamic acid (K
I
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. |
|---|---|
| AbstractList | 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, CO
2
+ H
2
O ⇋ HCO
3
−
+ H
+
with a k
cat
of 1.1 × 10
5
s
−1
and a k
cat
/K
m
of 7.58 × 10
6
M
−1
× s
−1
. This activity was inhibited by acetazolamide (K
I
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 (K
I
of 81 µM),
N,N
-diethyldithiocarbamate (K
I
of 67 µM) and sulphamic acid (K
I
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. A β-class carbonic anhydrase (CA, EC 4.2.1.1) was cloned from the genome of the Monogenean platyhelminth a parasite of Atlantic salmon. The new enzyme, GsaCAβ has a significant catalytic activity for the physiological reaction, CO + H O ⇋ HCO + H with a k of 1.1 × 10 s and a k /K of 7.58 × 10 M × s . This activity was inhibited by acetazolamide (K 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 (K of 81 µM), -diethyldithiocarbamate (K of 67 µM) and sulphamic acid (K 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. 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. 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, CO 2 + H 2 O ⇋ HCO 3 − + H + with a k cat of 1.1 × 10 5 s −1 and a k cat /K m of 7.58 × 10 6 M −1 × s −1 . This activity was inhibited by acetazolamide (K I 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 (K I of 81 µM), N,N-diethyldithiocarbamate (K I of 67 µM) and sulphamic acid (K I 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. |
| Author | Kuuslahti, Marianne Bonardi, Alessandro Tolvanen, Martti Barker, Harlan Lumme, Jaakko Tripathi, Amit Parkkila, Seppo Aisala, Heidi Supuran, Claudiu T. Primmer, Craig R. Zueva, Ksenia Aspatwar, Ashok |
| Author_xml | – sequence: 1 givenname: Ashok orcidid: 0000-0002-6938-7835 surname: Aspatwar fullname: Aspatwar, Ashok organization: Faculty of Medicine and Health Technology, Tampere University – sequence: 2 givenname: Harlan surname: Barker fullname: Barker, Harlan organization: Faculty of Medicine and Health Technology, Tampere University – sequence: 3 givenname: Heidi surname: Aisala fullname: Aisala, Heidi organization: Ecology and Genetics, University of Oulu – sequence: 4 givenname: Ksenia surname: Zueva fullname: Zueva, Ksenia organization: Department of Biology, University of Turku – sequence: 5 givenname: Marianne surname: Kuuslahti fullname: Kuuslahti, Marianne organization: Faculty of Medicine and Health Technology, Tampere University – sequence: 6 givenname: Martti surname: Tolvanen fullname: Tolvanen, Martti organization: Department of Computing, University of Turku – sequence: 7 givenname: Craig R. orcidid: 0000-0002-3687-8435 surname: Primmer fullname: Primmer, Craig R. organization: Institute of Biotechnology, Helsinki Institute of Life Science, University of Helsinki – sequence: 8 givenname: Jaakko surname: Lumme fullname: Lumme, Jaakko organization: Ecology and Genetics, University of Oulu – sequence: 9 givenname: Alessandro surname: Bonardi fullname: Bonardi, Alessandro organization: Department of Neuroscience, Psychology, Drug Research and Child's Health, Section of Pharmaceutical and Nutraceutical Sciences, University of Florence – sequence: 10 givenname: Amit surname: Tripathi fullname: Tripathi, Amit organization: Department of Zoology, University of Lucknow – sequence: 11 givenname: Seppo orcidid: 0000-0001-7323-8536 surname: Parkkila fullname: Parkkila, Seppo organization: Fimlab Ltd, Tampere University Hospital – sequence: 12 givenname: Claudiu T. orcidid: 0000-0003-4262-0323 surname: Supuran fullname: Supuran, Claudiu T. organization: Department of Neuroscience, Psychology, Drug Research and Child's Health, Section of Pharmaceutical and Nutraceutical Sciences, University of Florence |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35637617$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1080/14756366.2019.1571273 10.1016/j.bmc.2009.05.002 10.1016/j.molbiopara.2008.06.013 10.1080/14756366.2017.1332056 10.3390/metabo8020025 10.1042/BCJ20160115 10.1021/jm060807n 10.1080/14756366.2016.1221826 10.1016/j.ijpara.2014.04.003 10.3390/ijms22094324 10.1039/c2cc16395k 10.1016/j.bmc.2009.01.048 10.1021/acs.jmedchem.0c00733 10.1038/s41586-021-03819-2 10.1006/jmbi.2000.4315 10.1038/msb.2011.75 10.1038/nrd2467 10.1080/14756366.2020.1781845 10.1016/j.bmcl.2009.01.038 10.26508/lsa.201900429 10.3390/ijms21114175 10.1107/S2059798322000079 10.1080/13543784.2018.1548608 10.1002/bit.22962 10.1186/1471-2105-5-113 10.1186/s13071-015-1098-5 10.1016/j.jinorgbio.2011.11.017 10.1080/14756366.2020.1774572 10.1186/1756-3305-7-403 10.1016/j.jmb.2008.11.037 10.1016/j.bmcl.2008.07.122 10.1093/emboj/19.7.1407 10.1080/14756366.2018.1428572 10.2174/156802607780636753 10.1016/S0223-5234(97)86179-X 10.1093/molbev/msw046 10.1007/978-94-015-9956-6_26 10.1016/j.bmcl.2003.12.029 10.1093/oxfordjournals.molbev.a026334 10.1093/nar/gku316 10.1016/j.meegid.2021.104931 10.1186/s13071-016-1727-7 10.1017/S0031182099004436 10.1093/gbe/evu078 10.1186/1756-3305-7-38 10.1016/j.bmc.2008.12.035 10.1038/nmeth.4285 10.3389/fmicb.2021.629163 10.1042/CS20210040 10.1016/j.margen.2018.01.001 10.1080/14756366.2021.1882453 10.1080/17460441.2020.1743676 10.3390/ijms21051842 10.1080/14756366.2020.1867122 10.1021/jm300031j 10.1002/pro.3943 10.1021/acs.jmedchem.1c00840 10.1093/bioinformatics/btx431 10.1093/bioinformatics/btq461 10.1093/molbev/msu300 10.1016/j.bmc.2009.02.058 10.1002/med.21713 10.1038/s42003-019-0578-0 10.3390/molecules25112564 10.1021/jm011131t 10.1016/S0021-9258(18)62326-9 10.1016/j.bmc.2009.12.058 10.1016/j.bmcl.2004.06.073 10.1007/s00436-001-0587-y 10.1016/S0022-2836(05)80360-2 10.3109/14756366.2015.1122001 10.2174/138161210793429878 10.1186/1471-2091-11-28 10.3390/ijms222111583 |
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| Keywords | sulphamic acid Carbonic anhydrase Gyrodactylus salaris kinetics anion inhibitors |
| Language | English |
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| References | CIT0072 CIT0071 CIT0030 CIT0074 CIT0073 CIT0032 CIT0031 CIT0075 CIT0034 CIT0033 CIT0070 CIT0036 CIT0035 CIT0038 CIT0037 CIT0039 CIT0041 CIT0040 CIT0043 CIT0042 CIT0001 CIT0045 CIT0044 CIT0003 CIT0047 CIT0002 CIT0046 CIT0005 CIT0049 CIT0004 CIT0048 CIT0007 CIT0009 CIT0008 CIT0050 CIT0052 CIT0051 CIT0010 CIT0054 CIT0053 CIT0012 CIT0056 CIT0011 CIT0055 CIT0014 CIT0058 CIT0013 CIT0057 CIT0016 CIT0015 CIT0059 CIT0018 CIT0017 CIT0019 CIT0061 CIT0060 CIT0063 CIT0062 CIT0021 CIT0065 CIT0020 CIT0064 CIT0023 CIT0067 CIT0022 CIT0066 Schmahl G. (CIT0006) 1991; 38 CIT0025 CIT0069 CIT0024 CIT0068 CIT0027 CIT0026 CIT0029 CIT0028 |
| References_xml | – ident: CIT0031 doi: 10.1080/14756366.2019.1571273 – ident: CIT0057 doi: 10.1016/j.bmc.2009.05.002 – ident: CIT0025 doi: 10.1016/j.molbiopara.2008.06.013 – ident: CIT0073 doi: 10.1080/14756366.2017.1332056 – ident: CIT0016 doi: 10.3390/metabo8020025 – ident: CIT0010 doi: 10.1042/BCJ20160115 – ident: CIT0034 doi: 10.1021/jm060807n – ident: CIT0020 doi: 10.1080/14756366.2016.1221826 – ident: CIT0004 doi: 10.1016/j.ijpara.2014.04.003 – ident: CIT0066 doi: 10.3390/ijms22094324 – ident: CIT0075 doi: 10.1039/c2cc16395k – ident: CIT0027 doi: 10.1016/j.bmc.2009.01.048 – ident: CIT0036 doi: 10.1021/acs.jmedchem.0c00733 – ident: CIT0050 doi: 10.1038/s41586-021-03819-2 – ident: CIT0044 doi: 10.1006/jmbi.2000.4315 – ident: CIT0047 doi: 10.1038/msb.2011.75 – ident: CIT0014 doi: 10.1038/nrd2467 – ident: CIT0065 doi: 10.1080/14756366.2020.1781845 – ident: CIT0026 doi: 10.1016/j.bmcl.2009.01.038 – ident: CIT0045 doi: 10.26508/lsa.201900429 – ident: CIT0064 doi: 10.3390/ijms21114175 – volume: 38 start-page: 97 year: 1991 ident: CIT0006 publication-title: Folia Parasitol contributor: fullname: Schmahl G. – ident: CIT0024 doi: 10.1107/S2059798322000079 – ident: CIT0015 doi: 10.1080/13543784.2018.1548608 – ident: CIT0029 doi: 10.1002/bit.22962 – ident: CIT0039 doi: 10.1186/1471-2105-5-113 – ident: CIT0018 doi: 10.1186/s13071-015-1098-5 – ident: CIT0069 doi: 10.1016/j.jinorgbio.2011.11.017 – ident: CIT0032 doi: 10.1080/14756366.2020.1774572 – ident: CIT0019 doi: 10.1186/1756-3305-7-403 – ident: CIT0054 doi: 10.1016/j.jmb.2008.11.037 – ident: CIT0055 doi: 10.1016/j.bmcl.2008.07.122 – ident: CIT0051 doi: 10.1093/emboj/19.7.1407 – ident: CIT0070 doi: 10.1080/14756366.2018.1428572 – ident: CIT0062 doi: 10.2174/156802607780636753 – ident: CIT0037 doi: 10.1016/S0223-5234(97)86179-X – ident: CIT0043 doi: 10.1093/molbev/msw046 – ident: CIT0005 doi: 10.1007/978-94-015-9956-6_26 – ident: CIT0035 doi: 10.1016/j.bmcl.2003.12.029 – ident: CIT0040 doi: 10.1093/oxfordjournals.molbev.a026334 – ident: CIT0048 doi: 10.1093/nar/gku316 – ident: CIT0009 doi: 10.1016/j.meegid.2021.104931 – ident: CIT0003 doi: 10.1186/s13071-016-1727-7 – ident: CIT0007 doi: 10.1017/S0031182099004436 – ident: CIT0001 doi: 10.1093/gbe/evu078 – ident: CIT0053 doi: 10.1186/1756-3305-7-38 – ident: CIT0060 doi: 10.1016/j.bmc.2008.12.035 – ident: CIT0041 doi: 10.1038/nmeth.4285 – ident: CIT0067 doi: 10.3389/fmicb.2021.629163 – ident: CIT0011 doi: 10.1042/CS20210040 – ident: CIT0002 doi: 10.1016/j.margen.2018.01.001 – ident: CIT0017 doi: 10.1080/14756366.2021.1882453 – ident: CIT0013 doi: 10.1080/17460441.2020.1743676 – ident: CIT0022 doi: 10.3390/ijms21051842 – ident: CIT0033 doi: 10.1080/14756366.2020.1867122 – ident: CIT0074 doi: 10.1021/jm300031j – ident: CIT0049 doi: 10.1002/pro.3943 – ident: CIT0023 doi: 10.1021/acs.jmedchem.1c00840 – ident: CIT0046 doi: 10.1093/bioinformatics/btx431 – ident: CIT0038 doi: 10.1093/bioinformatics/btq461 – ident: CIT0042 doi: 10.1093/molbev/msu300 – ident: CIT0056 doi: 10.1016/j.bmc.2009.02.058 – ident: CIT0012 doi: 10.1002/med.21713 – ident: CIT0021 doi: 10.1038/s42003-019-0578-0 – ident: CIT0063 doi: 10.3390/molecules25112564 – ident: CIT0072 doi: 10.1021/jm011131t – ident: CIT0030 doi: 10.1016/S0021-9258(18)62326-9 – ident: CIT0058 doi: 10.1016/j.bmc.2009.12.058 – ident: CIT0061 doi: 10.1016/j.bmcl.2004.06.073 – ident: CIT0008 doi: 10.1007/s00436-001-0587-y – ident: CIT0028 doi: 10.1016/S0022-2836(05)80360-2 – ident: CIT0071 doi: 10.3109/14756366.2015.1122001 – ident: CIT0059 doi: 10.2174/138161210793429878 – ident: CIT0052 doi: 10.1186/1471-2091-11-28 – ident: CIT0068 doi: 10.3390/ijms222111583 |
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| Snippet | 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.... A β-class carbonic anhydrase (CA, EC 4.2.1.1) was cloned from the genome of the Monogenean platyhelminth a parasite of Atlantic salmon. The new enzyme, GsaCAβ... 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.... |
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| SubjectTerms | Acetazolamide Animals anion inhibitors Anions Anions - pharmacology Carbon dioxide Carbonic anhydrase Carbonic Anhydrase Inhibitors - pharmacology Carbonic anhydrases Carbonic Anhydrases - genetics Cloning Cloning, Molecular Enzymes Functional foods & nutraceuticals Genomes Glycerol Gyrodactylus salaris kinetics Neurosciences Original Parasites Parasites - genetics Platyhelminths - genetics Proteins Salmo salar - genetics Salmon Sulfamide Sulfonamides sulphamic acid Therapeutic targets |
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| Title | 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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