Cloning, purification, kinetic and anion inhibition studies of a recombinant ß-carbonic anhydrase from the Atlantic salmon parasite platyhelminth Gyrodactylus salaris.
J Enzyme Inhib Med Chem
; 37(1): 1577-1586, 2022 Dec.
Article
en En
| MEDLINE
| ID: mdl-35637617
ABSTRACT
A ß-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, GsaCAß has a significant catalytic activity for the physiological reaction, CO2 + H2O â 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 GsaCAß 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. GsaCAß is subsequently proposed as a new drug target for which effective inhibitors can be designed.
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Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Parásitos
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Platelmintos
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Anhidrasas Carbónicas
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Salmo salar
Idioma:
En
Revista:
J Enzyme Inhib Med Chem
Asunto de la revista:
BIOQUIMICA
/
QUIMICA
Año:
2022
Tipo del documento:
Article