Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporium.
Identifieur interne : 001052 ( Main/Exploration ); précédent : 001051; suivant : 001053Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporium.
Auteurs : V. Renganathan ; K. Miki ; M H GoldSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 1985.
Descripteurs français
- KwdFr :
- Analyse spectrale (MeSH), Basidiomycota (enzymologie), Isoenzymes (isolement et purification), Isoenzymes (métabolisme), Ligands (MeSH), Lignine (métabolisme), Masse moléculaire (MeSH), Oxygénases (antagonistes et inhibiteurs), Oxygénases (isolement et purification), Oxygénases (métabolisme), Peroxidases (MeSH), Peroxyde d'hydrogène (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Oxygénases.
- enzymologie : Basidiomycota.
- isolement et purification : Isoenzymes, Oxygénases.
- métabolisme : Isoenzymes, Lignine, Oxygénases, Peroxyde d'hydrogène.
- Analyse spectrale, Ligands, Masse moléculaire, Peroxidases.
English descriptors
- KwdEn :
- Basidiomycota (enzymology), Hydrogen Peroxide (metabolism), Isoenzymes (isolation & purification), Isoenzymes (metabolism), Ligands (MeSH), Lignin (metabolism), Molecular Weight (MeSH), Oxygenases (antagonists & inhibitors), Oxygenases (isolation & purification), Oxygenases (metabolism), Peroxidases (MeSH), Spectrum Analysis (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Oxygenases.
- chemical , isolation & purification : Isoenzymes, Oxygenases.
- chemical , metabolism : Hydrogen Peroxide, Isoenzymes, Lignin, Oxygenases.
- enzymology : Basidiomycota.
- chemical : Ligands, Molecular Weight, Peroxidases, Spectrum Analysis.
Abstract
Three different molecular forms of the H2O2-requiring heme enzyme, diarylpropane oxygenase, were isolated from the extracellular medium of Na-acetate buffered, agitated cultures of Phanerochaete chrysosporium. Forms I, II, and III were separated by DEAE-Sepharose and further purified on Sephadex G-100. Absorption maxima of the native, reduced, and a variety of ligand complexes of the three enzyme forms are essentially identical, indicating similar heme environments. All forms also have similar, but not identical, reactivity. The homogeneous proteins oxidized a diarylpropane, an olefin, a beta-aryl ether dimer, a phenylpropane, phenylpropane diols, and veratryl alcohol. Identical products were produced from each form. However, the specific activities of the three homogeneous enzymes for veratryl alcohol oxidation were 18.75, 11.80, and 8.48 mumol min-1 mg-1. In the presence of one equivalent of H2O2 the Soret maximum of diarylpropane oxygenase II shifted from 408 to 418 nm, and two additional maxima appeared at 526 and 553 nm, indicating the presence of an Fe(IV)-oxo species equivalent to horseradish peroxidase II. This oxidized species could be reduced back to the native form by veratryl alcohol and several reducing agents (e.g., Na2S2O4, NH2NH2, thiourea, or NADH). The molecular weights of diarylpropane oxygenases I, II, and III were approximately 39,000, 41,000, and 43,000, respectively. The major form (II) (85% of the activity) contained approximately 6% neutral carbohydrate. The affinity of the forms for concanavalin A-agarose suggests that they all are glycoenzymes.
DOI: 10.1016/0003-9861(85)90387-x
PubMed: 4026322
Affiliations:
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Le document en format XML
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Miki</name></author><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1985">1985</date><idno type="RBID">pubmed:4026322</idno><idno type="pmid">4026322</idno><idno type="doi">10.1016/0003-9861(85)90387-x</idno><idno type="wicri:Area/Main/Corpus">001049</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001049</idno><idno type="wicri:Area/Main/Curation">001049</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001049</idno><idno type="wicri:Area/Main/Exploration">001049</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporium.</title><author><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></author><author><name sortKey="Miki, K" sort="Miki, K" uniqKey="Miki K" first="K" last="Miki">K. Miki</name></author><author><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></author></analytic><series><title level="j">Archives of biochemistry and biophysics</title><idno type="ISSN">0003-9861</idno><imprint><date when="1985" type="published">1985</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term><term>Hydrogen Peroxide (metabolism)</term><term>Isoenzymes (isolation & purification)</term><term>Isoenzymes (metabolism)</term><term>Ligands (MeSH)</term><term>Lignin (metabolism)</term><term>Molecular Weight (MeSH)</term><term>Oxygenases (antagonists & inhibitors)</term><term>Oxygenases (isolation & purification)</term><term>Oxygenases (metabolism)</term><term>Peroxidases (MeSH)</term><term>Spectrum Analysis (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse spectrale (MeSH)</term><term>Basidiomycota (enzymologie)</term><term>Isoenzymes (isolement et purification)</term><term>Isoenzymes (métabolisme)</term><term>Ligands (MeSH)</term><term>Lignine (métabolisme)</term><term>Masse moléculaire (MeSH)</term><term>Oxygénases (antagonistes et inhibiteurs)</term><term>Oxygénases (isolement et purification)</term><term>Oxygénases (métabolisme)</term><term>Peroxidases (MeSH)</term><term>Peroxyde d'hydrogène (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Oxygenases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Isoenzymes</term><term>Oxygenases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Hydrogen Peroxide</term><term>Isoenzymes</term><term>Lignin</term><term>Oxygenases</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Oxygénases</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="isolement et purification" xml:lang="fr"><term>Isoenzymes</term><term>Oxygénases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Isoenzymes</term><term>Lignine</term><term>Oxygénases</term><term>Peroxyde d'hydrogène</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Ligands</term><term>Molecular Weight</term><term>Peroxidases</term><term>Spectrum Analysis</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse spectrale</term><term>Ligands</term><term>Masse moléculaire</term><term>Peroxidases</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Three different molecular forms of the H2O2-requiring heme enzyme, diarylpropane oxygenase, were isolated from the extracellular medium of Na-acetate buffered, agitated cultures of Phanerochaete chrysosporium. Forms I, II, and III were separated by DEAE-Sepharose and further purified on Sephadex G-100. Absorption maxima of the native, reduced, and a variety of ligand complexes of the three enzyme forms are essentially identical, indicating similar heme environments. All forms also have similar, but not identical, reactivity. The homogeneous proteins oxidized a diarylpropane, an olefin, a beta-aryl ether dimer, a phenylpropane, phenylpropane diols, and veratryl alcohol. Identical products were produced from each form. However, the specific activities of the three homogeneous enzymes for veratryl alcohol oxidation were 18.75, 11.80, and 8.48 mumol min-1 mg-1. In the presence of one equivalent of H2O2 the Soret maximum of diarylpropane oxygenase II shifted from 408 to 418 nm, and two additional maxima appeared at 526 and 553 nm, indicating the presence of an Fe(IV)-oxo species equivalent to horseradish peroxidase II. This oxidized species could be reduced back to the native form by veratryl alcohol and several reducing agents (e.g., Na2S2O4, NH2NH2, thiourea, or NADH). The molecular weights of diarylpropane oxygenases I, II, and III were approximately 39,000, 41,000, and 43,000, respectively. The major form (II) (85% of the activity) contained approximately 6% neutral carbohydrate. The affinity of the forms for concanavalin A-agarose suggests that they all are glycoenzymes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">4026322</PMID><DateCompleted><Year>1985</Year><Month>09</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>29</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>241</Volume><Issue>1</Issue><PubDate><Year>1985</Year><Month>Aug</Month><Day>15</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>304-14</MedlinePgn></Pagination><Abstract><AbstractText>Three different molecular forms of the H2O2-requiring heme enzyme, diarylpropane oxygenase, were isolated from the extracellular medium of Na-acetate buffered, agitated cultures of Phanerochaete chrysosporium. Forms I, II, and III were separated by DEAE-Sepharose and further purified on Sephadex G-100. Absorption maxima of the native, reduced, and a variety of ligand complexes of the three enzyme forms are essentially identical, indicating similar heme environments. All forms also have similar, but not identical, reactivity. The homogeneous proteins oxidized a diarylpropane, an olefin, a beta-aryl ether dimer, a phenylpropane, phenylpropane diols, and veratryl alcohol. Identical products were produced from each form. However, the specific activities of the three homogeneous enzymes for veratryl alcohol oxidation were 18.75, 11.80, and 8.48 mumol min-1 mg-1. In the presence of one equivalent of H2O2 the Soret maximum of diarylpropane oxygenase II shifted from 408 to 418 nm, and two additional maxima appeared at 526 and 553 nm, indicating the presence of an Fe(IV)-oxo species equivalent to horseradish peroxidase II. This oxidized species could be reduced back to the native form by veratryl alcohol and several reducing agents (e.g., Na2S2O4, NH2NH2, thiourea, or NADH). The molecular weights of diarylpropane oxygenases I, II, and III were approximately 39,000, 41,000, and 43,000, respectively. The major form (II) (85% of the activity) contained approximately 6% neutral carbohydrate. The affinity of the forms for concanavalin A-agarose suggests that they all are glycoenzymes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Renganathan</LastName><ForeName>V</ForeName><Initials>V</Initials></Author><Author ValidYN="Y"><LastName>Miki</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Gold</LastName><ForeName>M H</ForeName><Initials>MH</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008024">Ligands</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</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>EC 1.13.-</RegistryNumber><NameOfSubstance UI="D010105">Oxygenases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008024" MajorTopicYN="N">Ligands</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010105" MajorTopicYN="N">Oxygenases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="Y">Peroxidases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013057" MajorTopicYN="N">Spectrum Analysis</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1985</Year><Month>8</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1985</Year><Month>8</Month><Day>15</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1985</Year><Month>8</Month><Day>15</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">4026322</ArticleId><ArticleId IdType="pii">0003-9861(85)90387-X</ArticleId><ArticleId IdType="doi">10.1016/0003-9861(85)90387-x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name><name sortKey="Miki, K" sort="Miki, K" uniqKey="Miki K" first="K" last="Miki">K. Miki</name><name sortKey="Renganathan, V" sort="Renganathan, V" uniqKey="Renganathan V" first="V" last="Renganathan">V. Renganathan</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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