Exploration
Accueil
Racine
Exploration
Accueil

Serveur d'exploration sur la pourriture ligneuse

Attention, ce site est en cours de développement !
Attention, site généré par des moyens informatiques à partir de corpus bruts.
Les informations ne sont donc pas validées.

Stabilization of lignin peroxidases in white rot fungi by tryptophan.

Identifieur interne : 001C47 ( Main/Exploration ); précédent : 001C46; suivant : 001C48

Stabilization of lignin peroxidases in white rot fungi by tryptophan.

Auteurs : P J Collins [Irlande (pays)] ; J A Field ; P. Teunissen ; A D Dobson

Source :

RBID : pubmed:9212404

Descripteurs français

English descriptors

Abstract

Supplementation of various cultures of white rot fungi with tryptophan was found to have a large stimulatory effect on lignin peroxidase activity levels. This enhancement was greater than that observed in the presence of the lignin peroxidase recycling agent veratryl alcohol. Using reverse transcription-PCR, we found that tryptophan does not act to induce lignin peroxidase expression at the level of gene transcription. Instead, the activity enhancement observed is likely to result from the protective effect of tryptophan against H2O2 inactivation. In experiments using a partially purified lignin peroxidase preparation, tryptophan and its derivative indole were determined to function in the same way as veratryl alcohol in converting compound II, an oxidized form of lignin peroxidase, to ferric enzyme, thereby completing the catalytic cycle. Furthermore, tryptophan was found to be a better substrate for lignin peroxidase than veratryl alcohol. Inclusion of either tryptophan or indole enhanced the oxidation of the azo dyes methyl orange and Eriochrome blue black. Stimulation of azo dye oxidations by veratryl alcohol has previously been shown to be due to its enzyme recycling function. Our data allow us to propose that tryptophan stabilizes lignin peroxidase by acting as a reductant for the enzyme.

DOI: 10.1128/AEM.63.7.2543-2548.1997
PubMed: 9212404
PubMed Central: PMC168551


Affiliations:

Links toward previous steps (curation, corpus...)

Le document en format XML

<record>
<TEI>
<teiHeader>
<fileDesc>
<titleStmt>
<title xml:lang="en">Stabilization of lignin peroxidases in white rot fungi by tryptophan.</title>
<author>
<name sortKey="Collins, P J" sort="Collins, P J" uniqKey="Collins P" first="P J" last="Collins">P J Collins</name>
<affiliation wicri:level="1">
<nlm:affiliation>Microbiology Department, University College, Cork, Ireland.</nlm:affiliation>
<country xml:lang="fr">Irlande (pays)</country>
<wicri:regionArea>Microbiology Department, University College, Cork</wicri:regionArea>
<wicri:noRegion>Cork</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Field, J A" sort="Field, J A" uniqKey="Field J" first="J A" last="Field">J A Field</name>
</author>
<author>
<name sortKey="Teunissen, P" sort="Teunissen, P" uniqKey="Teunissen P" first="P" last="Teunissen">P. Teunissen</name>
</author>
<author>
<name sortKey="Dobson, A D" sort="Dobson, A D" uniqKey="Dobson A" first="A D" last="Dobson">A D Dobson</name>
</author>
</titleStmt>
<publicationStmt>
<idno type="wicri:source">PubMed</idno>
<date when="1997">1997</date>
<idno type="RBID">pubmed:9212404</idno>
<idno type="pmid">9212404</idno>
<idno type="pmc">PMC168551</idno>
<idno type="doi">10.1128/AEM.63.7.2543-2548.1997</idno>
<idno type="wicri:Area/Main/Corpus">001C57</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001C57</idno>
<idno type="wicri:Area/Main/Curation">001C57</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001C57</idno>
<idno type="wicri:Area/Main/Exploration">001C57</idno>
</publicationStmt>
<sourceDesc>
<biblStruct>
<analytic>
<title xml:lang="en">Stabilization of lignin peroxidases in white rot fungi by tryptophan.</title>
<author>
<name sortKey="Collins, P J" sort="Collins, P J" uniqKey="Collins P" first="P J" last="Collins">P J Collins</name>
<affiliation wicri:level="1">
<nlm:affiliation>Microbiology Department, University College, Cork, Ireland.</nlm:affiliation>
<country xml:lang="fr">Irlande (pays)</country>
<wicri:regionArea>Microbiology Department, University College, Cork</wicri:regionArea>
<wicri:noRegion>Cork</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Field, J A" sort="Field, J A" uniqKey="Field J" first="J A" last="Field">J A Field</name>
</author>
<author>
<name sortKey="Teunissen, P" sort="Teunissen, P" uniqKey="Teunissen P" first="P" last="Teunissen">P. Teunissen</name>
</author>
<author>
<name sortKey="Dobson, A D" sort="Dobson, A D" uniqKey="Dobson A" first="A D" last="Dobson">A D Dobson</name>
</author>
</analytic>
<series>
<title level="j">Applied and environmental microbiology</title>
<idno type="ISSN">0099-2240</idno>
<imprint>
<date when="1997" type="published">1997</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc>
<textClass>
<keywords scheme="KwdEn" xml:lang="en">
<term>Azo Compounds (metabolism)</term>
<term>Basidiomycota (enzymology)</term>
<term>Basidiomycota (genetics)</term>
<term>Basidiomycota (metabolism)</term>
<term>Benzyl Alcohols (metabolism)</term>
<term>Culture Media (metabolism)</term>
<term>Gene Expression Regulation, Enzymologic (MeSH)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Hydrogen Peroxide (metabolism)</term>
<term>Indoles (metabolism)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Peroxidases (genetics)</term>
<term>Peroxidases (metabolism)</term>
<term>Polymerase Chain Reaction (MeSH)</term>
<term>Transcription, Genetic (MeSH)</term>
<term>Tryptophan (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Alcools benzyliques (métabolisme)</term>
<term>Basidiomycota (enzymologie)</term>
<term>Basidiomycota (génétique)</term>
<term>Basidiomycota (métabolisme)</term>
<term>Composés azoïques (métabolisme)</term>
<term>Indoles (métabolisme)</term>
<term>Milieux de culture (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Peroxidases (génétique)</term>
<term>Peroxidases (métabolisme)</term>
<term>Peroxyde d'hydrogène (métabolisme)</term>
<term>Réaction de polymérisation en chaîne (MeSH)</term>
<term>Régulation de l'expression des gènes codant pour des enzymes (MeSH)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Transcription génétique (MeSH)</term>
<term>Tryptophane (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en">
<term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Azo Compounds</term>
<term>Benzyl Alcohols</term>
<term>Culture Media</term>
<term>Hydrogen Peroxide</term>
<term>Indoles</term>
<term>Peroxidases</term>
<term>Tryptophan</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr">
<term>Basidiomycota</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en">
<term>Basidiomycota</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Basidiomycota</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Basidiomycota</term>
<term>Peroxidases</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Basidiomycota</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Alcools benzyliques</term>
<term>Basidiomycota</term>
<term>Composés azoïques</term>
<term>Indoles</term>
<term>Milieux de culture</term>
<term>Peroxidases</term>
<term>Peroxyde d'hydrogène</term>
<term>Tryptophane</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Gene Expression Regulation, Enzymologic</term>
<term>Gene Expression Regulation, Fungal</term>
<term>Oxidation-Reduction</term>
<term>Polymerase Chain Reaction</term>
<term>Transcription, Genetic</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr">
<term>Oxydoréduction</term>
<term>Réaction de polymérisation en chaîne</term>
<term>Régulation de l'expression des gènes codant pour des enzymes</term>
<term>Régulation de l'expression des gènes fongiques</term>
<term>Transcription génétique</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">Supplementation of various cultures of white rot fungi with tryptophan was found to have a large stimulatory effect on lignin peroxidase activity levels. This enhancement was greater than that observed in the presence of the lignin peroxidase recycling agent veratryl alcohol. Using reverse transcription-PCR, we found that tryptophan does not act to induce lignin peroxidase expression at the level of gene transcription. Instead, the activity enhancement observed is likely to result from the protective effect of tryptophan against H2O2 inactivation. In experiments using a partially purified lignin peroxidase preparation, tryptophan and its derivative indole were determined to function in the same way as veratryl alcohol in converting compound II, an oxidized form of lignin peroxidase, to ferric enzyme, thereby completing the catalytic cycle. Furthermore, tryptophan was found to be a better substrate for lignin peroxidase than veratryl alcohol. Inclusion of either tryptophan or indole enhanced the oxidation of the azo dyes methyl orange and Eriochrome blue black. Stimulation of azo dye oxidations by veratryl alcohol has previously been shown to be due to its enzyme recycling function. Our data allow us to propose that tryptophan stabilizes lignin peroxidase by acting as a reductant for the enzyme.</div>
</front>
</TEI>
<pubmed>
<MedlineCitation Status="MEDLINE" Owner="NLM">
<PMID Version="1">9212404</PMID>
<DateCompleted>
<Year>1997</Year>
<Month>08</Month>
<Day>12</Day>
</DateCompleted>
<DateRevised>
<Year>2020</Year>
<Month>07</Month>
<Day>24</Day>
</DateRevised>
<Article PubModel="Print">
<Journal>
<ISSN IssnType="Print">0099-2240</ISSN>
<JournalIssue CitedMedium="Print">
<Volume>63</Volume>
<Issue>7</Issue>
<PubDate>
<Year>1997</Year>
<Month>Jul</Month>
</PubDate>
</JournalIssue>
<Title>Applied and environmental microbiology</Title>
<ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation>
</Journal>
<ArticleTitle>Stabilization of lignin peroxidases in white rot fungi by tryptophan.</ArticleTitle>
<Pagination>
<MedlinePgn>2543-8</MedlinePgn>
</Pagination>
<Abstract>
<AbstractText>Supplementation of various cultures of white rot fungi with tryptophan was found to have a large stimulatory effect on lignin peroxidase activity levels. This enhancement was greater than that observed in the presence of the lignin peroxidase recycling agent veratryl alcohol. Using reverse transcription-PCR, we found that tryptophan does not act to induce lignin peroxidase expression at the level of gene transcription. Instead, the activity enhancement observed is likely to result from the protective effect of tryptophan against H2O2 inactivation. In experiments using a partially purified lignin peroxidase preparation, tryptophan and its derivative indole were determined to function in the same way as veratryl alcohol in converting compound II, an oxidized form of lignin peroxidase, to ferric enzyme, thereby completing the catalytic cycle. Furthermore, tryptophan was found to be a better substrate for lignin peroxidase than veratryl alcohol. Inclusion of either tryptophan or indole enhanced the oxidation of the azo dyes methyl orange and Eriochrome blue black. Stimulation of azo dye oxidations by veratryl alcohol has previously been shown to be due to its enzyme recycling function. Our data allow us to propose that tryptophan stabilizes lignin peroxidase by acting as a reductant for the enzyme.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y">
<Author ValidYN="Y">
<LastName>Collins</LastName>
<ForeName>P J</ForeName>
<Initials>PJ</Initials>
<AffiliationInfo>
<Affiliation>Microbiology Department, University College, Cork, Ireland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Field</LastName>
<ForeName>J A</ForeName>
<Initials>JA</Initials>
</Author>
<Author ValidYN="Y">
<LastName>Teunissen</LastName>
<ForeName>P</ForeName>
<Initials>P</Initials>
</Author>
<Author ValidYN="Y">
<LastName>Dobson</LastName>
<ForeName>A D</ForeName>
<Initials>AD</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList>
<PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
</Article>
<MedlineJournalInfo>
<Country>United States</Country>
<MedlineTA>Appl Environ Microbiol</MedlineTA>
<NlmUniqueID>7605801</NlmUniqueID>
<ISSNLinking>0099-2240</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001391">Azo Compounds</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D003470">Culture Media</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007211">Indoles</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>6B4TC34456</RegistryNumber>
<NameOfSubstance UI="C100258">methyl orange</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>8724FJW4M5</RegistryNumber>
<NameOfSubstance UI="C030374">indole</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>8DUH1N11BX</RegistryNumber>
<NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>BBX060AN9V</RegistryNumber>
<NameOfSubstance UI="D006861">Hydrogen Peroxide</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>MB4T4A711H</RegistryNumber>
<NameOfSubstance UI="C042197">veratryl alcohol</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList>
<MeshHeading>
<DescriptorName UI="D001391" MajorTopicYN="N">Azo Compounds</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D003470" MajorTopicYN="N">Culture Media</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D015971" MajorTopicYN="N">Gene Expression Regulation, Enzymologic</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D007211" MajorTopicYN="N">Indoles</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D016133" MajorTopicYN="N">Polymerase Chain Reaction</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D014158" MajorTopicYN="N">Transcription, Genetic</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData>
<History>
<PubMedPubDate PubStatus="pubmed">
<Year>1997</Year>
<Month>7</Month>
<Day>1</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline">
<Year>1997</Year>
<Month>7</Month>
<Day>1</Day>
<Hour>0</Hour>
<Minute>1</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez">
<Year>1997</Year>
<Month>7</Month>
<Day>1</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList>
<ArticleId IdType="pubmed">9212404</ArticleId>
<ArticleId IdType="pmc">PMC168551</ArticleId>
<ArticleId IdType="doi">10.1128/AEM.63.7.2543-2548.1997</ArticleId>
</ArticleIdList>
<ReferenceList>
<Reference>
<Citation>Biochemistry. 1994 Apr 12;33(14):4225-30</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8155638</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochim Biophys Acta. 1994 Aug 2;1218(3):408-12</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8049266</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochemistry. 1996 Jan 9;35(1):102-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8555162</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):750-4</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">11607355</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1993 Jun 15;268(17):12274-81</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8509364</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Crit Rev Microbiol. 1987;15(2):141-68</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3322681</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochemistry. 1996 May 21;35(20):6418-24</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8639588</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochemistry. 1994 Nov 15;33(45):13349-54</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">7947743</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochem Biophys Res Commun. 1991 Aug 30;179(1):428-35</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">1883369</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Appl Environ Microbiol. 1993 Sep;59(9):2909-13</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8215363</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Appl Environ Microbiol. 1996 Apr;62(4):1151-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8919775</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1990 Jul 5;265(19):11137-42</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2162833</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Appl Environ Microbiol. 1988 Nov;54(11):2608-14</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16347765</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Rev Environ Contam Toxicol. 1994;138:49-72</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">7938784</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Science. 1983 Aug 12;221(4611):661-3</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">17787736</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Arch Biochem Biophys. 1993 Jan;300(1):57-62</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8424691</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1990 Feb 5;265(4):2070-7</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2298739</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Appl Environ Microbiol. 1988 Feb;54(2):466-72</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16347560</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>FEBS Lett. 1995 Sep 4;371(2):132-6</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">7672112</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Appl Environ Microbiol. 1996 Dec;62(12):4563-7</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16535468</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Annu Rev Microbiol. 1987;41:465-505</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3318677</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1988 Aug 5;263(22):10549-52</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3392025</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>FEBS Lett. 1996 Aug 5;391(1-2):144-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8706903</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochem Biophys Res Commun. 1991 Aug 15;178(3):1056-63</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">1872828</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Arch Biochem Biophys. 1990 May 15;279(1):158-66</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2337347</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1993 Feb 25;268(6):4429-40</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8440725</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochimie. 1992 Feb;74(2):177-82</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">1581393</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1995 Jul 14;270(28):16745-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">7622486</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Biochemistry. 1995 Dec 26;34(51):16860-9</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8527462</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Eur J Biochem. 1996 Apr 1;237(1):45-57</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">8620892</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Mol Cell Biol. 1989 Sep;9(9):3911-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2779571</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Appl Environ Microbiol. 1993 Dec;59(12):4031-6</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16349104</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1986 Dec 25;261(36):16948-52</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3023375</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations>
<list>
<country>
<li>Irlande (pays)</li>
</country>
</list>
<tree>
<noCountry>
<name sortKey="Dobson, A D" sort="Dobson, A D" uniqKey="Dobson A" first="A D" last="Dobson">A D Dobson</name>
<name sortKey="Field, J A" sort="Field, J A" uniqKey="Field J" first="J A" last="Field">J A Field</name>
<name sortKey="Teunissen, P" sort="Teunissen, P" uniqKey="Teunissen P" first="P" last="Teunissen">P. Teunissen</name>
</noCountry>
<country name="Irlande (pays)">
<noRegion>
<name sortKey="Collins, P J" sort="Collins, P J" uniqKey="Collins P" first="P J" last="Collins">P J Collins</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/WhiteRotV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001C47 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001C47 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    WhiteRotV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:9212404
   |texte=   Stabilization of lignin peroxidases in white rot fungi by tryptophan.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:9212404" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a WhiteRotV1
Wicri

This area was generated with Dilib version V0.6.37.
Data generation: Tue Nov 17 14:47:15 2020. Site generation: Tue Nov 17 14:50:18 2020