Inhibition of lignin peroxidase-mediated oxidation activity by ethylenediamine tetraacetic acid and N-N-N'-N'-tetramethylenediamine.
Identifieur interne : 000A38 ( Main/Exploration ); précédent : 000A37; suivant : 000A39Inhibition of lignin peroxidase-mediated oxidation activity by ethylenediamine tetraacetic acid and N-N-N'-N'-tetramethylenediamine.
Auteurs : H C Chang [États-Unis] ; J A BumpusSource :
- Proceedings of the National Science Council, Republic of China. Part B, Life sciences [ 0255-6596 ] ; 2001.
Descripteurs français
- KwdFr :
- Acide édétique (pharmacologie), Alcohol oxidoreductases (antagonistes et inhibiteurs), Alcohol oxidoreductases (métabolisme), Antienzymes (pharmacologie), Chélateurs (pharmacologie), DDT (métabolisme), Dépollution biologique de l'environnement (MeSH), Fixation compétitive (MeSH), Iodure de potassium (métabolisme), Iodure de potassium (pharmacologie), Oxydoréduction (MeSH), Peroxidases (antagonistes et inhibiteurs), Peroxidases (métabolisme), Phanerochaete (enzymologie), Protéines fongiques (antagonistes et inhibiteurs), Sites de fixation (MeSH), Zinc (pharmacologie), Éthylènediamines (pharmacologie).
- MESH :
- antagonistes et inhibiteurs : Alcohol oxidoreductases, Peroxidases, Protéines fongiques.
- enzymologie : Phanerochaete.
- métabolisme : Alcohol oxidoreductases, DDT, Iodure de potassium, Peroxidases.
- pharmacologie : Acide édétique, Antienzymes, Chélateurs, Iodure de potassium, Zinc, Éthylènediamines.
- Dépollution biologique de l'environnement, Fixation compétitive, Oxydoréduction, Sites de fixation.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (antagonists & inhibitors), Alcohol Oxidoreductases (metabolism), Binding Sites (MeSH), Binding, Competitive (MeSH), Biodegradation, Environmental (MeSH), Chelating Agents (pharmacology), DDT (metabolism), Edetic Acid (pharmacology), Enzyme Inhibitors (pharmacology), Ethylenediamines (pharmacology), Fungal Proteins (antagonists & inhibitors), Oxidation-Reduction (MeSH), Peroxidases (antagonists & inhibitors), Peroxidases (metabolism), Phanerochaete (enzymology), Potassium Iodide (metabolism), Potassium Iodide (pharmacology), Zinc (pharmacology).
- MESH :
- chemical , antagonists & inhibitors : Alcohol Oxidoreductases, Fungal Proteins, Peroxidases.
- chemical , metabolism : Alcohol Oxidoreductases, DDT, Peroxidases, Potassium Iodide.
- chemical , pharmacology : Chelating Agents, Edetic Acid, Enzyme Inhibitors, Ethylenediamines, Potassium Iodide, Zinc.
- enzymology : Phanerochaete.
- Binding Sites, Binding, Competitive, Biodegradation, Environmental, Oxidation-Reduction.
Abstract
The mineralization rate of LC-[1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane] (DDT) was reduced by 90% on the 18th day in fungal cultures of Phanerochaete chrysosporium in the presence of 8 mM ethylenediamine tetraacetic acid (EDTA). In the presence of 8 mM N-N-N'-N'-tetramethylenediamine (TEMED), the mineralization rate of 14C-DDT was reduced by 80%. In the presence of 2 mM or 10 mM EDTA, 95% inhibition of lignin peroxidase (LiP) mediated veratryl alcohol oxidase activity and 97% inhibition of LiP mediated iodide oxidase activity occurred. TEMED caused 79% inhibition of veratryl alcohol oxidase activity and 92% inhibition of iodide oxidase activity when the amount used was 2 mM and 10 mM, respectively. In the presence of Zn(II) with slight molar excess of the EDTA concentration, reversed the EDTA mediated non-competitive inhibition of LiP catalyzed veratryl alcohol or iodide oxidation, Zn(II) also reversed the inhibition of LiP catalyzed veratryl alcohol oxidase activity caused by chelators other than EDTA and TEMED. In addition to Zn(II), several other metal ions also relieved EDTA mediated inhibition of veratryl alcohol and iodide oxidase activity catalyzed by LiP. The ability of veratryl alcohol to inhibit iodide oxidation catalyzed by LiP showed that veratryl alcohol could inhibit LiP mediated iodide oxidase activity. Increasing the concentration of iodide was also shown to inhibit veratryl alcohol oxidation. Kinetic analysis showed that the reaction was competitive inhibition.
PubMed: 11254169
Affiliations:
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Part B, Life sciences</title><idno type="ISSN">0255-6596</idno><imprint><date when="2001" type="published">2001</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (antagonists & inhibitors)</term><term>Alcohol Oxidoreductases (metabolism)</term><term>Binding Sites (MeSH)</term><term>Binding, Competitive (MeSH)</term><term>Biodegradation, Environmental (MeSH)</term><term>Chelating Agents (pharmacology)</term><term>DDT (metabolism)</term><term>Edetic Acid (pharmacology)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Ethylenediamines (pharmacology)</term><term>Fungal Proteins (antagonists & inhibitors)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (antagonists & inhibitors)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Potassium Iodide (metabolism)</term><term>Potassium Iodide (pharmacology)</term><term>Zinc (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide édétique (pharmacologie)</term><term>Alcohol oxidoreductases (antagonistes et inhibiteurs)</term><term>Alcohol oxidoreductases (métabolisme)</term><term>Antienzymes (pharmacologie)</term><term>Chélateurs (pharmacologie)</term><term>DDT (métabolisme)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Fixation compétitive (MeSH)</term><term>Iodure de potassium (métabolisme)</term><term>Iodure de potassium (pharmacologie)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (antagonistes et inhibiteurs)</term><term>Peroxidases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Protéines fongiques (antagonistes et inhibiteurs)</term><term>Sites de fixation (MeSH)</term><term>Zinc (pharmacologie)</term><term>Éthylènediamines (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Fungal Proteins</term><term>Peroxidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>DDT</term><term>Peroxidases</term><term>Potassium Iodide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Chelating Agents</term><term>Edetic Acid</term><term>Enzyme Inhibitors</term><term>Ethylenediamines</term><term>Potassium Iodide</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Peroxidases</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>DDT</term><term>Iodure de potassium</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide édétique</term><term>Antienzymes</term><term>Chélateurs</term><term>Iodure de potassium</term><term>Zinc</term><term>Éthylènediamines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Binding, Competitive</term><term>Biodegradation, Environmental</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Dépollution biologique de l'environnement</term><term>Fixation compétitive</term><term>Oxydoréduction</term><term>Sites de fixation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The mineralization rate of LC-[1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane] (DDT) was reduced by 90% on the 18th day in fungal cultures of Phanerochaete chrysosporium in the presence of 8 mM ethylenediamine tetraacetic acid (EDTA). In the presence of 8 mM N-N-N'-N'-tetramethylenediamine (TEMED), the mineralization rate of 14C-DDT was reduced by 80%. In the presence of 2 mM or 10 mM EDTA, 95% inhibition of lignin peroxidase (LiP) mediated veratryl alcohol oxidase activity and 97% inhibition of LiP mediated iodide oxidase activity occurred. TEMED caused 79% inhibition of veratryl alcohol oxidase activity and 92% inhibition of iodide oxidase activity when the amount used was 2 mM and 10 mM, respectively. In the presence of Zn(II) with slight molar excess of the EDTA concentration, reversed the EDTA mediated non-competitive inhibition of LiP catalyzed veratryl alcohol or iodide oxidation, Zn(II) also reversed the inhibition of LiP catalyzed veratryl alcohol oxidase activity caused by chelators other than EDTA and TEMED. In addition to Zn(II), several other metal ions also relieved EDTA mediated inhibition of veratryl alcohol and iodide oxidase activity catalyzed by LiP. The ability of veratryl alcohol to inhibit iodide oxidation catalyzed by LiP showed that veratryl alcohol could inhibit LiP mediated iodide oxidase activity. Increasing the concentration of iodide was also shown to inhibit veratryl alcohol oxidation. Kinetic analysis showed that the reaction was competitive inhibition.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11254169</PMID><DateCompleted><Year>2001</Year><Month>06</Month><Day>28</Day></DateCompleted><DateRevised><Year>2015</Year><Month>09</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0255-6596</ISSN><JournalIssue CitedMedium="Print"><Volume>25</Volume><Issue>1</Issue><PubDate><Year>2001</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Proceedings of the National Science Council, Republic of China. Part B, Life sciences</Title><ISOAbbreviation>Proc Natl Sci Counc Repub China B</ISOAbbreviation></Journal><ArticleTitle>Inhibition of lignin peroxidase-mediated oxidation activity by ethylenediamine tetraacetic acid and N-N-N'-N'-tetramethylenediamine.</ArticleTitle><Pagination><MedlinePgn>26-33</MedlinePgn></Pagination><Abstract><AbstractText>The mineralization rate of LC-[1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane] (DDT) was reduced by 90% on the 18th day in fungal cultures of Phanerochaete chrysosporium in the presence of 8 mM ethylenediamine tetraacetic acid (EDTA). In the presence of 8 mM N-N-N'-N'-tetramethylenediamine (TEMED), the mineralization rate of 14C-DDT was reduced by 80%. In the presence of 2 mM or 10 mM EDTA, 95% inhibition of lignin peroxidase (LiP) mediated veratryl alcohol oxidase activity and 97% inhibition of LiP mediated iodide oxidase activity occurred. TEMED caused 79% inhibition of veratryl alcohol oxidase activity and 92% inhibition of iodide oxidase activity when the amount used was 2 mM and 10 mM, respectively. In the presence of Zn(II) with slight molar excess of the EDTA concentration, reversed the EDTA mediated non-competitive inhibition of LiP catalyzed veratryl alcohol or iodide oxidation, Zn(II) also reversed the inhibition of LiP catalyzed veratryl alcohol oxidase activity caused by chelators other than EDTA and TEMED. In addition to Zn(II), several other metal ions also relieved EDTA mediated inhibition of veratryl alcohol and iodide oxidase activity catalyzed by LiP. The ability of veratryl alcohol to inhibit iodide oxidation catalyzed by LiP showed that veratryl alcohol could inhibit LiP mediated iodide oxidase activity. Increasing the concentration of iodide was also shown to inhibit veratryl alcohol oxidation. Kinetic analysis showed that the reaction was competitive inhibition.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>H C</ForeName><Initials>HC</Initials><AffiliationInfo><Affiliation>Division of Biochemical Toxicology, National Center for Toxicology Research, Food and Drug Administration, Jefferson, AR, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bumpus</LastName><ForeName>J A</ForeName><Initials>JA</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>ESO 4492</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>China (Republic : 1949- )</Country><MedlineTA>Proc Natl 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Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>CIW5S16655</RegistryNumber><NameOfSubstance UI="D003634">DDT</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.-</RegistryNumber><NameOfSubstance UI="C057990">veratryl alcohol oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>J41CSQ7QDS</RegistryNumber><NameOfSubstance UI="D015032">Zinc</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000037" 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MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005029" MajorTopicYN="N">Ethylenediamines</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011193" MajorTopicYN="N">Potassium Iodide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015032" MajorTopicYN="N">Zinc</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>3</Month><Day>20</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>6</Month><Day>29</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>3</Month><Day>20</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11254169</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Arkansas</li></region></list><tree><noCountry><name sortKey="Bumpus, J A" sort="Bumpus, J A" uniqKey="Bumpus J" first="J A" last="Bumpus">J A Bumpus</name></noCountry><country name="États-Unis"><region name="Arkansas"><name sortKey="Chang, H C" sort="Chang, H C" uniqKey="Chang H" first="H C" last="Chang">H C Chang</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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