Characterization of the gene encoding manganese peroxidase isozyme 3 from Phanerochaete chrysosporium.
Identifieur interne : 000C19 ( Main/Exploration ); précédent : 000C18; suivant : 000C20Characterization of the gene encoding manganese peroxidase isozyme 3 from Phanerochaete chrysosporium.
Auteurs : M. Alic [États-Unis] ; L. Akileswaran ; M H GoldSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 1997.
Descripteurs français
- KwdFr :
- Basidiomycota (enzymologie), Basidiomycota (génétique), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Exons (MeSH), Introns (MeSH), Isoenzymes (biosynthèse), Isoenzymes (génétique), Peroxidases (biosynthèse), Peroxidases (composition chimique), Peroxidases (génétique), Protéines recombinantes (biosynthèse), Protéines recombinantes (composition chimique), Régions promotrices (génétique) (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Séquences d'acides nucléiques régulatrices (MeSH), Transcription génétique (MeSH).
- MESH :
- biosynthèse : Isoenzymes, Peroxidases, Protéines recombinantes.
- composition chimique : Peroxidases, Protéines recombinantes.
- enzymologie : Basidiomycota.
- génétique : Basidiomycota, Isoenzymes, Peroxidases.
- Clonage moléculaire, Données de séquences moléculaires, Exons, Introns, Régions promotrices (génétique), Séquence d'acides aminés, Séquence nucléotidique, Séquences d'acides nucléiques régulatrices, Transcription génétique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Basidiomycota (enzymology), Basidiomycota (genetics), Cloning, Molecular (MeSH), Exons (MeSH), Introns (MeSH), Isoenzymes (biosynthesis), Isoenzymes (genetics), Molecular Sequence Data (MeSH), Peroxidases (biosynthesis), Peroxidases (chemistry), Peroxidases (genetics), Promoter Regions, Genetic (MeSH), Recombinant Proteins (biosynthesis), Recombinant Proteins (chemistry), Regulatory Sequences, Nucleic Acid (MeSH), Transcription, Genetic (MeSH).
- MESH :
- chemical , biosynthesis : Isoenzymes, Peroxidases, Recombinant Proteins.
- chemical , chemistry : Peroxidases, Recombinant Proteins.
- enzymology : Basidiomycota.
- genetics : Basidiomycota, Isoenzymes, Peroxidases.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Exons, Introns, Molecular Sequence Data, Promoter Regions, Genetic, Regulatory Sequences, Nucleic Acid, Transcription, Genetic.
Abstract
The gene encoding manganese peroxidase isozyme 3 (MnP3) from the white-rot basidiomycete Phanerochaete chrysosporium was cloned and sequenced. The mnp3 gene encodes a mature protein of 357 amino acids with a 25 amino-acid signal peptide. The amino acids involved in peroxidase function, as well as those forming the MnII binding site and those involved in disulfide bond formation, are conserved in the MnP3 sequence. The mnp3 gene has six introns, indicating that the sequenced P. chrysosporium mnp genes can be divided into three subfamilies on the basis of intron-exon structure. The mnp3 gene promoter contains putative metal response elements and heat shock elements which may be involved in the regulation of mnp gene transcription by Mn, the substrate for the enzyme, and by heat shock.
DOI: 10.1016/s0167-4838(96)00235-x
PubMed: 9074609
Affiliations:
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Akileswaran</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="1997">1997</date><idno type="RBID">pubmed:9074609</idno><idno type="pmid">9074609</idno><idno type="doi">10.1016/s0167-4838(96)00235-x</idno><idno type="wicri:Area/Main/Corpus">000C18</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C18</idno><idno type="wicri:Area/Main/Curation">000C18</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C18</idno><idno type="wicri:Area/Main/Exploration">000C18</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Characterization of the gene encoding manganese peroxidase isozyme 3 from Phanerochaete chrysosporium.</title><author><name sortKey="Alic, M" sort="Alic, M" uniqKey="Alic M" first="M" last="Alic">M. Alic</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000</wicri:regionArea><placeName><settlement type="city">Portland</settlement><region type="state">Oregon</region></placeName></affiliation></author><author><name sortKey="Akileswaran, L" sort="Akileswaran, L" uniqKey="Akileswaran L" first="L" last="Akileswaran">L. 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The mnp3 gene encodes a mature protein of 357 amino acids with a 25 amino-acid signal peptide. The amino acids involved in peroxidase function, as well as those forming the MnII binding site and those involved in disulfide bond formation, are conserved in the MnP3 sequence. The mnp3 gene has six introns, indicating that the sequenced P. chrysosporium mnp genes can be divided into three subfamilies on the basis of intron-exon structure. The mnp3 gene promoter contains putative metal response elements and heat shock elements which may be involved in the regulation of mnp gene transcription by Mn, the substrate for the enzyme, and by heat shock.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9074609</PMID><DateCompleted><Year>1997</Year><Month>04</Month><Day>14</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>10</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1338</Volume><Issue>1</Issue><PubDate><Year>1997</Year><Month>Mar</Month><Day>07</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Characterization of the gene encoding manganese peroxidase isozyme 3 from Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>1-7</MedlinePgn></Pagination><Abstract><AbstractText>The gene encoding manganese peroxidase isozyme 3 (MnP3) from the white-rot basidiomycete Phanerochaete chrysosporium was cloned and sequenced. The mnp3 gene encodes a mature protein of 357 amino acids with a 25 amino-acid signal peptide. The amino acids involved in peroxidase function, as well as those forming the MnII binding site and those involved in disulfide bond formation, are conserved in the MnP3 sequence. The mnp3 gene has six introns, indicating that the sequenced P. chrysosporium mnp genes can be divided into three subfamilies on the basis of intron-exon structure. The mnp3 gene promoter contains putative metal response elements and heat shock elements which may be involved in the regulation of mnp gene transcription by Mn, the substrate for the enzyme, and by heat shock.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Alic</LastName><ForeName>M</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Akileswaran</LastName><ForeName>L</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Gold</LastName><ForeName>M H</ForeName><Initials>MH</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>U70998</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><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="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005091" MajorTopicYN="N">Exons</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007438" MajorTopicYN="N">Introns</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011401" MajorTopicYN="Y">Promoter Regions, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012045" MajorTopicYN="N">Regulatory Sequences, Nucleic Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014158" MajorTopicYN="N">Transcription, Genetic</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1997</Year><Month>3</Month><Day>7</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1997</Year><Month>3</Month><Day>7</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1997</Year><Month>3</Month><Day>7</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9074609</ArticleId><ArticleId IdType="pii">S0167-4838(96)00235-X</ArticleId><ArticleId IdType="doi">10.1016/s0167-4838(96)00235-x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Oregon</li></region><settlement><li>Portland</li></settlement></list><tree><noCountry><name sortKey="Akileswaran, L" sort="Akileswaran, L" uniqKey="Akileswaran L" first="L" last="Akileswaran">L. Akileswaran</name><name sortKey="Gold, M H" sort="Gold, M H" uniqKey="Gold M" first="M H" last="Gold">M H Gold</name></noCountry><country name="États-Unis"><region name="Oregon"><name sortKey="Alic, M" sort="Alic, M" uniqKey="Alic M" first="M" last="Alic">M. Alic</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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