Characterization and inhibition studies of an α-carbonic anhydrase from the endangered sturgeon species Acipenser gueldenstaedti.
Identifieur interne : 000334 ( PubMed/Corpus ); précédent : 000333; suivant : 000335Characterization and inhibition studies of an α-carbonic anhydrase from the endangered sturgeon species Acipenser gueldenstaedti.
Auteurs : Sevgi Kolayli ; 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
Links to Exploration step
pubmed:21381885Le document en format XML
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Supuran</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21381885</idno><idno type="pmid">21381885</idno><idno type="doi">10.3109/14756366.2011.554415</idno><idno type="wicri:Area/PubMed/Corpus">000334</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000334</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Characterization and inhibition studies of an α-carbonic anhydrase from the endangered sturgeon species Acipenser gueldenstaedti.</title><author><name sortKey="Kolayli, Sevgi" sort="Kolayli, Sevgi" uniqKey="Kolayli S" first="Sevgi" last="Kolayli">Sevgi Kolayli</name><affiliation><nlm:affiliation>Department of Chemistry, Faculty of Arts and Sciences, Karadeniz Technical University, Trabzon, Turkey.</nlm:affiliation></affiliation></author><author><name sortKey="Karahalil, Fatma" sort="Karahalil, Fatma" uniqKey="Karahalil F" first="Fatma" last="Karahalil">Fatma Karahalil</name></author><author><name sortKey="Sahin, Huseyin" sort="Sahin, Huseyin" uniqKey="Sahin H" first="Huseyin" last="Sahin">Huseyin Sahin</name></author><author><name sortKey="Dincer, Barbaros" sort="Dincer, Barbaros" uniqKey="Dincer B" first="Barbaros" last="Dincer">Barbaros Dincer</name></author><author><name sortKey="Supuran, Claudiu T" sort="Supuran, Claudiu T" uniqKey="Supuran C" first="Claudiu T" last="Supuran">Claudiu T. 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><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21381885</PMID><DateCreated><Year>2011</Year><Month>11</Month><Day>17</Day></DateCreated><DateCompleted><Year>2012</Year><Month>06</Month><Day>08</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1475-6374</ISSN><JournalIssue CitedMedium="Internet"><Volume>26</Volume><Issue>6</Issue><PubDate><Year>2011</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Journal of enzyme inhibition and medicinal chemistry</Title><ISOAbbreviation>J Enzyme Inhib Med Chem</ISOAbbreviation></Journal><ArticleTitle>Characterization and inhibition studies of an α-carbonic anhydrase from the endangered sturgeon species Acipenser gueldenstaedti.</ArticleTitle><Pagination><MedlinePgn>895-900</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3109/14756366.2011.554415</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kolayli</LastName><ForeName>Sevgi</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Faculty of Arts and Sciences, Karadeniz Technical University, Trabzon, Turkey.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Karahalil</LastName><ForeName>Fatma</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Sahin</LastName><ForeName>Huseyin</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Dincer</LastName><ForeName>Barbaros</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Supuran</LastName><ForeName>Claudiu T</ForeName><Initials>CT</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal 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UI="D056727" MajorTopicYN="N">Endangered Species</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004912" MajorTopicYN="N">Erythrocytes</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005399" MajorTopicYN="Y">Fishes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010575" MajorTopicYN="N">Pesticides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000494" 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