Characterization and inhibition studies of an α-carbonic anhydrase from the endangered sturgeon species Acipenser gueldenstaedti.
Identifieur interne : 000605 ( Main/Merge ); précédent : 000604; suivant : 000606Characterization and inhibition studies of an α-carbonic anhydrase from the endangered sturgeon species Acipenser gueldenstaedti.
Auteurs : Sevgi Kolayli [Turquie] ; Fatma Karahalil ; Huseyin Sahin ; Barbaros Dincer ; Claudiu T. SupuranSource :
- Journal of enzyme inhibition and medicinal chemistry [ 1475-6374 ] ; 2011.
English descriptors
- KwdEn :
- Acetazolamide (chemistry), Acetazolamide (pharmacology), Animals, Carbonic Anhydrases (isolation & purification), Carbonic Anhydrases (metabolism), Dose-Response Relationship, Drug, Endangered Species, Enzyme Inhibitors (chemistry), Enzyme Inhibitors (pharmacology), Erythrocytes (enzymology), Fishes, Humans, Kinetics, Pesticides (chemistry), Pesticides (pharmacology), Structure-Activity Relationship, Sulfanilamides (chemistry), Sulfanilamides (pharmacology).
- MESH :
- chemical , chemistry : Acetazolamide, Enzyme Inhibitors, Pesticides, Sulfanilamides.
- chemical , isolation & purification : Carbonic Anhydrases.
- chemical , metabolism : Carbonic Anhydrases.
- chemical , pharmacology : Acetazolamide, Enzyme Inhibitors, Pesticides, Sulfanilamides.
- enzymology : Erythrocytes.
- Animals, Dose-Response Relationship, Drug, Endangered Species, Fishes, Humans, Kinetics, Structure-Activity Relationship.
Abstract
An α-carbonic anhydrase (CA, EC 4.2.1.1) was purified and characterized kinetically from erythrocytes of the sturgeon Acipenser gueldenstaedti, an endangered species. The sturgeon enzyme (AgCA) showed kinetic parameters for the CO(2) hydration reaction comparable with those of the human erythrocytes enzyme hCA II, being a highly active enzyme, whereas its esterase activity with 4-nitrophenyl acetate as substrate was lower. Sulphonamide inhibitors (acetazolamide, sulphanilamide) strongly inhibited AgCA, whereas metal ions (Ag(+), Zn(2+), Cu(2+) and Co(2+)) were weak, millimolar inhibitors. Several widely used pesticides (2,4-dichlorophenol, dithiocarbamates, parathion and carbaryl) were also assayed as inhibitors of this enzyme. The dithiocarbamates were low micromolar AgCA inhibitors (IC(50) of 16-18 μM), whereas the other pesticides inhibited the enzyme with IC(50)s in the range of 102-398 μM. The wide use of dithiocarbamate pesticides may be one of the factors enhancing the vulnerability of this sturgeon species to pollutants.
DOI: 10.3109/14756366.2011.554415
PubMed: 21381885
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Supuran</name></author></analytic><series><title level="j">Journal of enzyme inhibition and medicinal chemistry</title><idno type="eISSN">1475-6374</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acetazolamide (chemistry)</term><term>Acetazolamide (pharmacology)</term><term>Animals</term><term>Carbonic Anhydrases (isolation & purification)</term><term>Carbonic Anhydrases (metabolism)</term><term>Dose-Response Relationship, Drug</term><term>Endangered Species</term><term>Enzyme Inhibitors (chemistry)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Erythrocytes (enzymology)</term><term>Fishes</term><term>Humans</term><term>Kinetics</term><term>Pesticides (chemistry)</term><term>Pesticides (pharmacology)</term><term>Structure-Activity Relationship</term><term>Sulfanilamides (chemistry)</term><term>Sulfanilamides (pharmacology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Acetazolamide</term><term>Enzyme Inhibitors</term><term>Pesticides</term><term>Sulfanilamides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Carbonic Anhydrases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbonic Anhydrases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Acetazolamide</term><term>Enzyme Inhibitors</term><term>Pesticides</term><term>Sulfanilamides</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Erythrocytes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Dose-Response Relationship, Drug</term><term>Endangered Species</term><term>Fishes</term><term>Humans</term><term>Kinetics</term><term>Structure-Activity Relationship</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">An α-carbonic anhydrase (CA, EC 4.2.1.1) was purified and characterized kinetically from erythrocytes of the sturgeon Acipenser gueldenstaedti, an endangered species. The sturgeon enzyme (AgCA) showed kinetic parameters for the CO(2) hydration reaction comparable with those of the human erythrocytes enzyme hCA II, being a highly active enzyme, whereas its esterase activity with 4-nitrophenyl acetate as substrate was lower. Sulphonamide inhibitors (acetazolamide, sulphanilamide) strongly inhibited AgCA, whereas metal ions (Ag(+), Zn(2+), Cu(2+) and Co(2+)) were weak, millimolar inhibitors. Several widely used pesticides (2,4-dichlorophenol, dithiocarbamates, parathion and carbaryl) were also assayed as inhibitors of this enzyme. The dithiocarbamates were low micromolar AgCA inhibitors (IC(50) of 16-18 μM), whereas the other pesticides inhibited the enzyme with IC(50)s in the range of 102-398 μM. The wide use of dithiocarbamate pesticides may be one of the factors enhancing the vulnerability of this sturgeon species to pollutants.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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