Kinetics of inhibition of isoproturon to glutathione-associated enzymes in wheat.
Identifieur interne : 000100 ( Main/Corpus ); précédent : 000099; suivant : 000101Kinetics of inhibition of isoproturon to glutathione-associated enzymes in wheat.
Auteurs : Nemat M. Hassan ; Mamdouh M. Nemat AllaSource :
- Physiology and molecular biology of plants : an international journal of functional plant biology [ 0971-5894 ] ; 2020.
Abstract
The present study aimed at investigating the kinetic of inhibition of isoproturon to the GSH-associated enzymes [γ-glutamyl-cysteine synthetase (γ-GCS), glutathione synthetase (GS), glutathione reductase (GR), glutathione-S-transferase (GST) and glutathione peroxidase (GPX)] in wheat. Isoproturon, applied to 10-day-old seedlings for the following 12 days, provoked significant reductions in shoot fresh and dry weights, protein, thiols and glutathione (GSH); however, oxidized glutathione (GSSG) was elevated while GSH/GSSG ratio was declined with concomitant significant inhibitions in the activities of γ-GCS, GS, GR, GST and GPX; the effect was time dependent. IC50 and Ki values of isoproturon were lowest for GPX, highest for both GST and GR, and moderate for both γ-GCS and GS. The herbicide markedly decreased Vmax of γ-GCS, GS and GPX but unchanged that of GST and GR; however, Km of γ-GCS, GS, GST and GR increased but unchanged for GPX. The pattern of response of changing Vmax, Km, Vmax/Km, kcat and kcat/Km for in vivo and in vitro tests of each enzyme seemed most likely similar. These results indicate that a malfunction to defense system was induced in wheat by isoproturon resulting in inhibitions in GSH-associated enzymes, the magnitude of inhibition was most pronounced in GPX followed by γ-GCS, GS, GST, and GR. These findings could conclude that isoproturon competitively inhibited GST and GR; however, the inhibition was noncompetitive for GPX but mixed for both γ-GCS and GS.
DOI: 10.1007/s12298-020-00812-3
PubMed: 32647464
PubMed Central: PMC7326839
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pubmed:32647464Le document en format XML
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<author><name sortKey="Hassan, Nemat M" sort="Hassan, Nemat M" uniqKey="Hassan N" first="Nemat M" last="Hassan">Nemat M. Hassan</name>
<affiliation><nlm:affiliation>Botany Department, Faculty of Science, Damietta University, PO 34517, New Damietta, Egypt.</nlm:affiliation>
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<author><name sortKey="Nemat Alla, Mamdouh M" sort="Nemat Alla, Mamdouh M" uniqKey="Nemat Alla M" first="Mamdouh M" last="Nemat Alla">Mamdouh M. Nemat Alla</name>
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<front><div type="abstract" xml:lang="en">The present study aimed at investigating the kinetic of inhibition of isoproturon to the GSH-associated enzymes [γ-glutamyl-cysteine synthetase (γ-GCS), glutathione synthetase (GS), glutathione reductase (GR), glutathione-S-transferase (GST) and glutathione peroxidase (GPX)] in wheat. Isoproturon, applied to 10-day-old seedlings for the following 12 days, provoked significant reductions in shoot fresh and dry weights, protein, thiols and glutathione (GSH); however, oxidized glutathione (GSSG) was elevated while GSH/GSSG ratio was declined with concomitant significant inhibitions in the activities of γ-GCS, GS, GR, GST and GPX; the effect was time dependent. IC50 and Ki values of isoproturon were lowest for GPX, highest for both GST and GR, and moderate for both γ-GCS and GS. The herbicide markedly decreased Vmax of γ-GCS, GS and GPX but unchanged that of GST and GR; however, Km of γ-GCS, GS, GST and GR increased but unchanged for GPX. The pattern of response of changing Vmax, Km, Vmax/Km, kcat and kcat/Km for in vivo and in vitro tests of each enzyme seemed most likely similar. These results indicate that a malfunction to defense system was induced in wheat by isoproturon resulting in inhibitions in GSH-associated enzymes, the magnitude of inhibition was most pronounced in GPX followed by γ-GCS, GS, GST, and GR. These findings could conclude that isoproturon competitively inhibited GST and GR; however, the inhibition was noncompetitive for GPX but mixed for both γ-GCS and GS.</div>
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<ArticleTitle>Kinetics of inhibition of isoproturon to glutathione-associated enzymes in wheat.</ArticleTitle>
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<Abstract><AbstractText>The present study aimed at investigating the kinetic of inhibition of isoproturon to the GSH-associated enzymes [γ-glutamyl-cysteine synthetase (γ-GCS), glutathione synthetase (GS), glutathione reductase (GR), glutathione-S-transferase (GST) and glutathione peroxidase (GPX)] in wheat. Isoproturon, applied to 10-day-old seedlings for the following 12 days, provoked significant reductions in shoot fresh and dry weights, protein, thiols and glutathione (GSH); however, oxidized glutathione (GSSG) was elevated while GSH/GSSG ratio was declined with concomitant significant inhibitions in the activities of γ-GCS, GS, GR, GST and GPX; the effect was time dependent. IC50 and Ki values of isoproturon were lowest for GPX, highest for both GST and GR, and moderate for both γ-GCS and GS. The herbicide markedly decreased Vmax of γ-GCS, GS and GPX but unchanged that of GST and GR; however, Km of γ-GCS, GS, GST and GR increased but unchanged for GPX. The pattern of response of changing Vmax, Km, Vmax/Km, kcat and kcat/Km for in vivo and in vitro tests of each enzyme seemed most likely similar. These results indicate that a malfunction to defense system was induced in wheat by isoproturon resulting in inhibitions in GSH-associated enzymes, the magnitude of inhibition was most pronounced in GPX followed by γ-GCS, GS, GST, and GR. These findings could conclude that isoproturon competitively inhibited GST and GR; however, the inhibition was noncompetitive for GPX but mixed for both γ-GCS and GS.</AbstractText>
<CopyrightInformation>© Prof. H.S. Srivastava Foundation for Science and Society 2020.</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hassan</LastName>
<ForeName>Nemat M</ForeName>
<Initials>NM</Initials>
<Identifier Source="ORCID">0000-0003-0441-0595</Identifier>
<AffiliationInfo><Affiliation>Botany Department, Faculty of Science, Damietta University, PO 34517, New Damietta, Egypt.</Affiliation>
<Identifier Source="GRID">grid.462079.e</Identifier>
<Identifier Source="ISNI">0000 0004 4699 2981</Identifier>
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<Author ValidYN="Y"><LastName>Nemat Alla</LastName>
<ForeName>Mamdouh M</ForeName>
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<AffiliationInfo><Affiliation>Botany Department, Faculty of Science, Damietta University, PO 34517, New Damietta, Egypt.</Affiliation>
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<Month>06</Month>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Glutathione</Keyword>
<Keyword MajorTopicYN="N">Glutathione-associated enzymes</Keyword>
<Keyword MajorTopicYN="N">Isoproturon</Keyword>
<Keyword MajorTopicYN="N">Kinetic</Keyword>
<Keyword MajorTopicYN="N">Wheat</Keyword>
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<CoiStatement>Conflict of interestThe authors declare that they have no conflict of interest.</CoiStatement>
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