A novel type of peroxidase gene from the white-rot fungus Trametes versicolor.
Identifieur interne : 000D71 ( Main/Exploration ); précédent : 000D70; suivant : 000D72A novel type of peroxidase gene from the white-rot fungus Trametes versicolor.
Auteurs : L. Jönsson [Suède] ; H G Becker ; P O NymanSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 1994.
Descripteurs français
- KwdFr :
- ADN fongique (composition chimique), Alignement de séquences (MeSH), Champignons (enzymologie), Champignons (génétique), Données de séquences moléculaires (MeSH), Introns (MeSH), Isoenzymes (composition chimique), Isoenzymes (génétique), Myeloperoxidase (composition chimique), Myeloperoxidase (génétique), Peroxidases (composition chimique), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : ADN fongique, Isoenzymes, Myeloperoxidase, Peroxidases.
- enzymologie : Champignons.
- génétique : Champignons, Isoenzymes, Myeloperoxidase.
- Alignement de séquences, Données de séquences moléculaires, Introns, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), DNA, Fungal (chemistry), Fungi (enzymology), Fungi (genetics), Introns (MeSH), Isoenzymes (chemistry), Isoenzymes (genetics), Molecular Sequence Data (MeSH), Peroxidase (chemistry), Peroxidase (genetics), Peroxidases (chemistry), Sequence Alignment (MeSH).
- MESH :
- chemical , chemistry : DNA, Fungal, Isoenzymes, Peroxidase, Peroxidases.
- enzymology : Fungi.
- genetics : Fungi, Isoenzymes, Peroxidase.
- Amino Acid Sequence, Base Sequence, Introns, Molecular Sequence Data, Sequence Alignment.
Abstract
The wood-decaying fungus Trametes versicolor secretes a large number of peroxidase isozymes, presumed to partake in the degradation of lignin. From enzymic studies, two types of peroxidases have been distinguished: lignin peroxidases and manganese peroxidases. We here report the finding of a T. versicolor peroxidase gene, PG V, which displays several features not observed in previously studied peroxidase genes from white-rot fungi, such as a high number of introns (12). Eight of the 12 introns have positions equivalent to introns of peroxidase genes from another white-rot fungus, Phanerochaete chrysosporium. The gene structure of PG V appears to be primarily related to known lignin peroxidase genes, while the encoded mature 339-residue protein has several characteristics in common with manganese peroxidases. Analyses further indicate that PG V encodes a Ser instead of an Asn at a position regarded as invariant within the enzyme superfamily, with the side chain involved in hydrogen bonding with the distal His.
DOI: 10.1016/0167-4838(94)00083-2
PubMed: 8075158
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Jönsson</name><affiliation wicri:level="1"><nlm:affiliation>Chemical Center, University of Lund, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Chemical Center, University of Lund</wicri:regionArea><wicri:noRegion>University of Lund</wicri:noRegion></affiliation></author><author><name sortKey="Becker, H G" sort="Becker, H G" uniqKey="Becker H" first="H G" last="Becker">H G Becker</name></author><author><name sortKey="Nyman, P O" sort="Nyman, P O" uniqKey="Nyman P" first="P O" last="Nyman">P O Nyman</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1994">1994</date><idno type="RBID">pubmed:8075158</idno><idno type="pmid">8075158</idno><idno type="doi">10.1016/0167-4838(94)00083-2</idno><idno type="wicri:Area/Main/Corpus">000D41</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000D41</idno><idno type="wicri:Area/Main/Curation">000D41</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000D41</idno><idno type="wicri:Area/Main/Exploration">000D41</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A novel type of peroxidase gene from the white-rot fungus Trametes versicolor.</title><author><name sortKey="Jonsson, L" sort="Jonsson, L" uniqKey="Jonsson L" first="L" last="Jönsson">L. 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From enzymic studies, two types of peroxidases have been distinguished: lignin peroxidases and manganese peroxidases. We here report the finding of a T. versicolor peroxidase gene, PG V, which displays several features not observed in previously studied peroxidase genes from white-rot fungi, such as a high number of introns (12). Eight of the 12 introns have positions equivalent to introns of peroxidase genes from another white-rot fungus, Phanerochaete chrysosporium. The gene structure of PG V appears to be primarily related to known lignin peroxidase genes, while the encoded mature 339-residue protein has several characteristics in common with manganese peroxidases. Analyses further indicate that PG V encodes a Ser instead of an Asn at a position regarded as invariant within the enzyme superfamily, with the side chain involved in hydrogen bonding with the distal His.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8075158</PMID><DateCompleted><Year>1994</Year><Month>10</Month><Day>04</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>1207</Volume><Issue>2</Issue><PubDate><Year>1994</Year><Month>Aug</Month><Day>17</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>A novel type of peroxidase gene from the white-rot fungus Trametes versicolor.</ArticleTitle><Pagination><MedlinePgn>255-9</MedlinePgn></Pagination><Abstract><AbstractText>The wood-decaying fungus Trametes versicolor secretes a large number of peroxidase isozymes, presumed to partake in the degradation of lignin. From enzymic studies, two types of peroxidases have been distinguished: lignin peroxidases and manganese peroxidases. We here report the finding of a T. versicolor peroxidase gene, PG V, which displays several features not observed in previously studied peroxidase genes from white-rot fungi, such as a high number of introns (12). Eight of the 12 introns have positions equivalent to introns of peroxidase genes from another white-rot fungus, Phanerochaete chrysosporium. The gene structure of PG V appears to be primarily related to known lignin peroxidase genes, while the encoded mature 339-residue protein has several characteristics in common with manganese peroxidases. 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