Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation.
Identifieur interne : 000D80 ( Main/Exploration ); précédent : 000D79; suivant : 000D81Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation.
Auteurs : I C Kuan [États-Unis] ; M. TienSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 1993.
Descripteurs français
- KwdFr :
- Agaricales (croissance et développement), Agaricales (effets des médicaments et des substances chimiques), Agaricales (enzymologie), Cinétique (MeSH), Dépollution biologique de l'environnement (MeSH), Lignine (métabolisme), Oxalates (métabolisme), Oxalates (pharmacologie), Oxidoreductases (métabolisme), Peroxidases (métabolisme).
- MESH :
- croissance et développement : Agaricales.
- effets des médicaments et des substances chimiques : Agaricales.
- enzymologie : Agaricales.
- métabolisme : Lignine, Oxalates, Oxidoreductases, Peroxidases.
- pharmacologie : Oxalates.
- Cinétique, Dépollution biologique de l'environnement.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Lignin, Oxalates, Oxidoreductases, Peroxidases.
- drug effects : Agaricales.
- enzymology : Agaricales.
- growth & development : Agaricales.
- chemical , pharmacology : Oxalates.
- Biodegradation, Environmental, Kinetics.
Abstract
Oxalate is produced by numerous wood-degrading fungi. Our studies here show that the white-rot fungus Phanerochaete chrysosporium produces extracellular oxalate under conditions that induce synthesis of the ligninolytic system. Little or no oxalate was detected in cultures grown under high nutrient nitrogen or carbon. This extracellular oxalate was identified and quantitated by HPLC. Its identity was further substantiated by its decomposition by the enzyme oxalate oxidase. The oxalate content of the extracellular fluid (peaking at 60 microM) paralleled the extracellular activity of the lignin-degrading enzyme, Mn peroxidase. Significantly, we demonstrated that oxalate, at physiological concentrations, substantially stimulated Mn peroxidase-catalyzed phenol red oxidation, presumably by its ability to chelate Mn. Stopped flow studies also indicate that oxalate accelerates the turnover of Mn peroxidase. Furthermore, we discovered that oxalate can support Mn peroxidase-catalyzed oxidations in the absence of exogenous H2O2 and in the presence of dioxygen. These results allow us to propose an important role for oxalate, a ubiquitous compound produced by wood-destroying fungi, in lignin biodegradation.
DOI: 10.1073/pnas.90.4.1242
PubMed: 8433984
PubMed Central: PMC45848
Affiliations:
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Tien</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="1993" type="published">1993</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Agaricales (drug effects)</term><term>Agaricales (enzymology)</term><term>Agaricales (growth & development)</term><term>Biodegradation, Environmental (MeSH)</term><term>Kinetics (MeSH)</term><term>Lignin (metabolism)</term><term>Oxalates (metabolism)</term><term>Oxalates (pharmacology)</term><term>Oxidoreductases (metabolism)</term><term>Peroxidases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agaricales (croissance et développement)</term><term>Agaricales (effets des médicaments et des substances chimiques)</term><term>Agaricales (enzymologie)</term><term>Cinétique (MeSH)</term><term>Dépollution biologique de l'environnement (MeSH)</term><term>Lignine (métabolisme)</term><term>Oxalates (métabolisme)</term><term>Oxalates (pharmacologie)</term><term>Oxidoreductases (métabolisme)</term><term>Peroxidases (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Lignin</term><term>Oxalates</term><term>Oxidoreductases</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Lignine</term><term>Oxalates</term><term>Oxidoreductases</term><term>Peroxidases</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Oxalates</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Oxalates</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biodegradation, Environmental</term><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Dépollution biologique de l'environnement</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Oxalate is produced by numerous wood-degrading fungi. Our studies here show that the white-rot fungus Phanerochaete chrysosporium produces extracellular oxalate under conditions that induce synthesis of the ligninolytic system. Little or no oxalate was detected in cultures grown under high nutrient nitrogen or carbon. This extracellular oxalate was identified and quantitated by HPLC. Its identity was further substantiated by its decomposition by the enzyme oxalate oxidase. The oxalate content of the extracellular fluid (peaking at 60 microM) paralleled the extracellular activity of the lignin-degrading enzyme, Mn peroxidase. Significantly, we demonstrated that oxalate, at physiological concentrations, substantially stimulated Mn peroxidase-catalyzed phenol red oxidation, presumably by its ability to chelate Mn. Stopped flow studies also indicate that oxalate accelerates the turnover of Mn peroxidase. Furthermore, we discovered that oxalate can support Mn peroxidase-catalyzed oxidations in the absence of exogenous H2O2 and in the presence of dioxygen. These results allow us to propose an important role for oxalate, a ubiquitous compound produced by wood-destroying fungi, in lignin biodegradation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8433984</PMID><DateCompleted><Year>1993</Year><Month>03</Month><Day>16</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>90</Volume><Issue>4</Issue><PubDate><Year>1993</Year><Month>Feb</Month><Day>15</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation.</ArticleTitle><Pagination><MedlinePgn>1242-6</MedlinePgn></Pagination><Abstract><AbstractText>Oxalate is produced by numerous wood-degrading fungi. Our studies here show that the white-rot fungus Phanerochaete chrysosporium produces extracellular oxalate under conditions that induce synthesis of the ligninolytic system. Little or no oxalate was detected in cultures grown under high nutrient nitrogen or carbon. This extracellular oxalate was identified and quantitated by HPLC. Its identity was further substantiated by its decomposition by the enzyme oxalate oxidase. The oxalate content of the extracellular fluid (peaking at 60 microM) paralleled the extracellular activity of the lignin-degrading enzyme, Mn peroxidase. Significantly, we demonstrated that oxalate, at physiological concentrations, substantially stimulated Mn peroxidase-catalyzed phenol red oxidation, presumably by its ability to chelate Mn. Stopped flow studies also indicate that oxalate accelerates the turnover of Mn peroxidase. Furthermore, we discovered that oxalate can support Mn peroxidase-catalyzed oxidations in the absence of exogenous H2O2 and in the presence of dioxygen. These results allow us to propose an important role for oxalate, a ubiquitous compound produced by wood-destroying fungi, in lignin biodegradation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kuan</LastName><ForeName>I C</ForeName><Initials>IC</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tien</LastName><ForeName>M</ForeName><Initials>M</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>1-P42ES04922-01</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, 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Pennsylvanie</li></orgName></list><tree><noCountry><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. Tien</name></noCountry><country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Kuan, I C" sort="Kuan, I C" uniqKey="Kuan I" first="I C" last="Kuan">I C Kuan</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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