Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system.
Identifieur interne : 000F23 ( Main/Exploration ); précédent : 000F22; suivant : 000F24Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system.
Auteurs : E A Pease ; S D Aust ; M. TienSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1991.
Descripteurs français
- KwdFr :
- ADN fongique (analyse), Baculoviridae (génétique), Chrysosporium (enzymologie), Expression des gènes (MeSH), Isoenzymes (génétique), Masse moléculaire (MeSH), Maturation post-traductionnelle des protéines (MeSH), Peroxidases (biosynthèse), Peroxidases (génétique), Point isoélectrique (MeSH), Protéines recombinantes (biosynthèse), Protéines recombinantes (génétique), Spécificité du substrat (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- analyse : ADN fongique.
- biosynthèse : Peroxidases, Protéines recombinantes.
- enzymologie : Chrysosporium.
- génétique : Baculoviridae, Isoenzymes, Peroxidases, Protéines recombinantes.
- Expression des gènes, Masse moléculaire, Maturation post-traductionnelle des protéines, Point isoélectrique, Spécificité du substrat, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Baculoviridae (genetics), Chrysosporium (enzymology), DNA, Fungal (analysis), Electrophoresis, Polyacrylamide Gel (MeSH), Gene Expression (MeSH), Isoelectric Point (MeSH), Isoenzymes (genetics), Molecular Weight (MeSH), Peroxidases (biosynthesis), Peroxidases (genetics), Protein Processing, Post-Translational (MeSH), Recombinant Proteins (biosynthesis), Recombinant Proteins (genetics), Substrate Specificity (MeSH).
- MESH :
- chemical , analysis : DNA, Fungal.
- chemical , biosynthesis : Peroxidases, Recombinant Proteins.
- enzymology : Chrysosporium.
- genetics : Baculoviridae, Isoenzymes, Peroxidases, Recombinant Proteins.
- Electrophoresis, Polyacrylamide Gel, Gene Expression, Isoelectric Point, Molecular Weight, Protein Processing, Post-Translational, Substrate Specificity.
Abstract
The cDNA encoding Mn peroxidase isozyme H4 from Phanerochaete chrysosporium was recombined into a baculovirus and heterologously expressed in Sf9 cells. The recombinant Mn peroxidase has the same molecular weight as the native enzyme as determined by SDS-PAGE and cross-reacts with a Mn peroxidase-specific antibody. The recombinant enzyme has a slightly lower pI than the native fungal isozyme H4 indicating some differences in post-translational modification. Phenol red, guaiacol, and vanillylacetone, substrates of the native Mn peroxidase, are oxidized by the recombinant enzyme. All of the activities are dependent on both Mn (II) and H2O2.
DOI: 10.1016/0006-291x(91)91903-p
PubMed: 1898410
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Tien</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:1898410</idno><idno type="pmid">1898410</idno><idno type="doi">10.1016/0006-291x(91)91903-p</idno><idno type="wicri:Area/Main/Corpus">000F03</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000F03</idno><idno type="wicri:Area/Main/Curation">000F03</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000F03</idno><idno type="wicri:Area/Main/Exploration">000F03</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system.</title><author><name sortKey="Pease, E A" sort="Pease, E A" uniqKey="Pease E" first="E A" last="Pease">E A Pease</name><affiliation><nlm:affiliation>Department of Molecular and Cell Biology, Pennsylvania State University University Park 16802.</nlm:affiliation><wicri:noCountry code="subField">Pennsylvania State University University Park 16802</wicri:noCountry></affiliation></author><author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></author><author><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. 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The recombinant Mn peroxidase has the same molecular weight as the native enzyme as determined by SDS-PAGE and cross-reacts with a Mn peroxidase-specific antibody. The recombinant enzyme has a slightly lower pI than the native fungal isozyme H4 indicating some differences in post-translational modification. Phenol red, guaiacol, and vanillylacetone, substrates of the native Mn peroxidase, are oxidized by the recombinant enzyme. All of the activities are dependent on both Mn (II) and H2O2.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1898410</PMID><DateCompleted><Year>1991</Year><Month>10</Month><Day>22</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>179</Volume><Issue>2</Issue><PubDate><Year>1991</Year><Month>Sep</Month><Day>16</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Heterologous expression of active manganese peroxidase from Phanerochaete chrysosporium using the baculovirus expression system.</ArticleTitle><Pagination><MedlinePgn>897-903</MedlinePgn></Pagination><Abstract><AbstractText>The cDNA encoding Mn peroxidase isozyme H4 from Phanerochaete chrysosporium was recombined into a baculovirus and heterologously expressed in Sf9 cells. The recombinant Mn peroxidase has the same molecular weight as the native enzyme as determined by SDS-PAGE and cross-reacts with a Mn peroxidase-specific antibody. The recombinant enzyme has a slightly lower pI than the native fungal isozyme H4 indicating some differences in post-translational modification. Phenol red, guaiacol, and vanillylacetone, substrates of the native Mn peroxidase, are oxidized by the recombinant enzyme. All of the activities are dependent on both Mn (II) and H2O2.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pease</LastName><ForeName>E A</ForeName><Initials>EA</Initials><AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, Pennsylvania State University University Park 16802.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aust</LastName><ForeName>S D</ForeName><Initials>SD</Initials></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, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004271">DNA, Fungal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D016367" MajorTopicYN="N">Baculoviridae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002912" MajorTopicYN="N">Chrysosporium</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004271" MajorTopicYN="N">DNA, Fungal</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007526" MajorTopicYN="N">Isoelectric Point</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="N">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>9</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>9</Month><Day>16</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>9</Month><Day>16</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1898410</ArticleId><ArticleId IdType="pii">0006-291X(91)91903-P</ArticleId><ArticleId IdType="doi">10.1016/0006-291x(91)91903-p</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list></list><tree><noCountry><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name><name sortKey="Pease, E A" sort="Pease, E A" uniqKey="Pease E" first="E A" last="Pease">E A Pease</name><name sortKey="Tien, M" sort="Tien, M" uniqKey="Tien M" first="M" last="Tien">M. 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