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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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Kinetics of inhibition of isoproturon to glutathione-associated enzymes in wheat.</title><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></affiliation></author><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><affiliation><nlm:affiliation>Botany Department, Faculty of Science, Damietta University, PO 34517, New Damietta, Egypt.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32647464</idno><idno type="pmid">32647464</idno><idno type="doi">10.1007/s12298-020-00812-3</idno><idno type="pmc">PMC7326839</idno><idno type="wicri:Area/Main/Corpus">000100</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000100</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Kinetics of inhibition of isoproturon to glutathione-associated enzymes in wheat.</title><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></affiliation></author><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><affiliation><nlm:affiliation>Botany Department, Faculty of Science, Damietta University, PO 34517, New Damietta, Egypt.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Physiology and molecular biology of plants : an international journal of functional plant biology</title><idno type="ISSN">0971-5894</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><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></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">32647464</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0971-5894</ISSN><JournalIssue CitedMedium="Print"><Volume>26</Volume><Issue>7</Issue><PubDate><Year>2020</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Physiology and molecular biology of plants : an international journal of functional plant biology</Title><ISOAbbreviation>Physiol Mol Biol Plants</ISOAbbreviation></Journal><ArticleTitle>Kinetics of inhibition of isoproturon to glutathione-associated enzymes in wheat.</ArticleTitle><Pagination><MedlinePgn>1505-1518</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s12298-020-00812-3</ELocationID><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></Abstract><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></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nemat Alla</LastName><ForeName>Mamdouh M</ForeName><Initials>MM</Initials><Identifier Source="ORCID">0000-0002-6161-0449</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></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>06</Month><Day>11</Day></ArticleDate></Article><MedlineJournalInfo><Country>India</Country><MedlineTA>Physiol Mol Biol Plants</MedlineTA><NlmUniqueID>101304333</NlmUniqueID><ISSNLinking>0974-0430</ISSNLinking></MedlineJournalInfo><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></KeywordList><CoiStatement>Conflict of interestThe authors declare that they have no conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate 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IdType="pmc">PMC7326839</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Plant Physiol. 1991 May;96(1):104-9</Citation><ArticleIdList><ArticleId IdType="pubmed">16668137</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Direct. 2019 Feb 18;3(2):e00119</Citation><ArticleIdList><ArticleId IdType="pubmed">31245762</ArticleId></ArticleIdList></Reference><Reference><Citation>J Theor Biol. 2006 Feb 21;238(4):919-36</Citation><ArticleIdList><ArticleId IdType="pubmed">16125728</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1970 Aug 15;227(5259):680-5</Citation><ArticleIdList><ArticleId IdType="pubmed">5432063</ArticleId></ArticleIdList></Reference><Reference><Citation>Physiol Mol Biol Plants. 2017 Apr;23(2):249-268</Citation><ArticleIdList><ArticleId IdType="pubmed">28461715</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem J. 1975 Jun;147(3):513-22</Citation><ArticleIdList><ArticleId IdType="pubmed">810139</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1988 Dec;175(2):408-13</Citation><ArticleIdList><ArticleId IdType="pubmed">3239770</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2001 Mar 9;1546(1):242-52</Citation><ArticleIdList><ArticleId IdType="pubmed">11257527</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Sci. 2001 Jan 5;160(2):291-299</Citation><ArticleIdList><ArticleId IdType="pubmed">11164601</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1968 Oct 24;25(1):192-205</Citation><ArticleIdList><ArticleId IdType="pubmed">4973948</ArticleId></ArticleIdList></Reference><Reference><Citation>Trends Biochem Sci. 2001 Nov;26(11):648-53</Citation><ArticleIdList><ArticleId IdType="pubmed">11701322</ArticleId></ArticleIdList></Reference><Reference><Citation>Chem Biol Interact. 2002 Apr 20;140(1):49-65</Citation><ArticleIdList><ArticleId IdType="pubmed">12044560</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol Biochem. 2005 Feb;43(2):107-16</Citation><ArticleIdList><ArticleId IdType="pubmed">15820657</ArticleId></ArticleIdList></Reference><Reference><Citation>Biotechniques. 2011 Sep;51(3):193-4</Citation><ArticleIdList><ArticleId IdType="pubmed">21906042</ArticleId></ArticleIdList></Reference><Reference><Citation>Exp Parasitol. 2005 Oct;111(2):137-41</Citation><ArticleIdList><ArticleId IdType="pubmed">16087176</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1986 Oct;82(2):351-6</Citation><ArticleIdList><ArticleId IdType="pubmed">16665034</ArticleId></ArticleIdList></Reference><Reference><Citation>Sci Rep. 2017 Jun 6;7(1):2879</Citation><ArticleIdList><ArticleId IdType="pubmed">28588258</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9785-90</Citation><ArticleIdList><ArticleId IdType="pubmed">12909715</ArticleId></ArticleIdList></Reference><Reference><Citation>Environ Toxicol Pharmacol. 2006 Jul;22(1):27-34</Citation><ArticleIdList><ArticleId IdType="pubmed">21783682</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1976 May 7;72:248-54</Citation><ArticleIdList><ArticleId IdType="pubmed">942051</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochim Biophys Acta. 2012 Jan;1817(1):182-93</Citation><ArticleIdList><ArticleId IdType="pubmed">21565154</ArticleId></ArticleIdList></Reference><Reference><Citation>J Agric Food Chem. 2008 Jun 25;56(12):4825-31</Citation><ArticleIdList><ArticleId IdType="pubmed">18522406</ArticleId></ArticleIdList></Reference><Reference><Citation>Physiol Plant. 2004 Mar;120(3):421-433</Citation><ArticleIdList><ArticleId IdType="pubmed">15032839</ArticleId></ArticleIdList></Reference><Reference><Citation>J Enzyme Inhib Med Chem. 2009 Dec;24(6):1288-90</Citation><ArticleIdList><ArticleId IdType="pubmed">19912063</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell Physiol. 2005 Apr;46(4):557-62</Citation><ArticleIdList><ArticleId IdType="pubmed">15695431</ArticleId></ArticleIdList></Reference><Reference><Citation>Protoplasma. 2015 May;252(3):835-44</Citation><ArticleIdList><ArticleId IdType="pubmed">25344655</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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