The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases.
Identifieur interne : 000A65 ( Main/Exploration ); précédent : 000A64; suivant : 000A66The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases.
Auteurs : S. Camarero [Espagne] ; F J Ruiz-Due As ; S. Sarkar ; M J Martínez ; A T MartínezSource :
- FEMS microbiology letters [ 0378-1097 ] ; 2000.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Analyse de séquence d'ADN (MeSH), Cellulose (métabolisme), Champignons (enzymologie), Champignons (génétique), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Gènes fongiques (MeSH), Lignine (métabolisme), Milieux de culture (MeSH), Myeloperoxidase (composition chimique), Myeloperoxidase (génétique), Myeloperoxidase (métabolisme), Pleurotus (croissance et développement), Pleurotus (enzymologie), Pleurotus (génétique), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Myeloperoxidase.
- croissance et développement : Pleurotus.
- enzymologie : Champignons, Pleurotus.
- génétique : Champignons, Myeloperoxidase, Pleurotus.
- métabolisme : Cellulose, Lignine, Myeloperoxidase.
- Alignement de séquences, Analyse de séquence d'ADN, Clonage moléculaire, Données de séquences moléculaires, Gènes fongiques, Milieux de culture, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cellulose (metabolism), Cloning, Molecular (MeSH), Culture Media (MeSH), Fungi (enzymology), Fungi (genetics), Genes, Fungal (MeSH), Lignin (metabolism), Molecular Sequence Data (MeSH), Peroxidase (chemistry), Peroxidase (genetics), Peroxidase (metabolism), Pleurotus (enzymology), Pleurotus (genetics), Pleurotus (growth & development), Sequence Alignment (MeSH), Sequence Analysis, DNA (MeSH).
- MESH :
- chemical , chemistry : Peroxidase.
- chemical , genetics : Peroxidase.
- chemical , metabolism : Cellulose, Lignin, Peroxidase.
- enzymology : Fungi, Pleurotus.
- genetics : Fungi, Pleurotus.
- growth & development : Pleurotus.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Culture Media, Genes, Fungal, Molecular Sequence Data, Sequence Alignment, Sequence Analysis, DNA.
Abstract
We report cloning and sequencing of gene ps1 encoding a versatile peroxidase combining catalytic properties of lignin peroxidase (LiP) and manganese peroxidase (MnP) isolated from lignocellulose cultures of the white-rot fungus Pleurotus eryngii. The gene contains 15 putative introns, and the deduced amino acid sequence consists of a 339-residue mature protein with a 31-residue signal peptide. Several putative response elements were identified in the promoter region. Amino acid residues involved in oxidation of Mn(2+) and aromatic substrates by direct electron transfer to heme and long-range electron transfer from superficial residues as predicted by analogy with Phanerochaete chrysosporium MnP and LiP, respectively. A dendrogram is presented illustrating sequence relationships between 29 fungal peroxidases.
DOI: 10.1111/j.1574-6968.2000.tb09316.x
PubMed: 11004397
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Sarkar</name></author><author><name sortKey="Martinez, M J" sort="Martinez, M J" uniqKey="Martinez M" first="M J" last="Martínez">M J Martínez</name></author><author><name sortKey="Martinez, A T" sort="Martinez, A T" uniqKey="Martinez A" first="A T" last="Martínez">A T Martínez</name></author></analytic><series><title level="j">FEMS microbiology letters</title><idno type="ISSN">0378-1097</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Cellulose (metabolism)</term><term>Cloning, Molecular (MeSH)</term><term>Culture Media (MeSH)</term><term>Fungi (enzymology)</term><term>Fungi (genetics)</term><term>Genes, Fungal (MeSH)</term><term>Lignin (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Peroxidase (chemistry)</term><term>Peroxidase (genetics)</term><term>Peroxidase (metabolism)</term><term>Pleurotus (enzymology)</term><term>Pleurotus (genetics)</term><term>Pleurotus (growth & development)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Analysis, DNA (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Analyse de séquence d'ADN (MeSH)</term><term>Cellulose (métabolisme)</term><term>Champignons (enzymologie)</term><term>Champignons (génétique)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Gènes fongiques (MeSH)</term><term>Lignine (métabolisme)</term><term>Milieux de culture (MeSH)</term><term>Myeloperoxidase (composition chimique)</term><term>Myeloperoxidase (génétique)</term><term>Myeloperoxidase (métabolisme)</term><term>Pleurotus (croissance et développement)</term><term>Pleurotus (enzymologie)</term><term>Pleurotus (génétique)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Peroxidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulose</term><term>Lignin</term><term>Peroxidase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Myeloperoxidase</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Champignons</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Fungi</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Champignons</term><term>Myeloperoxidase</term><term>Pleurotus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellulose</term><term>Lignine</term><term>Myeloperoxidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Culture Media</term><term>Genes, Fungal</term><term>Molecular Sequence Data</term><term>Sequence Alignment</term><term>Sequence Analysis, DNA</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Analyse de séquence d'ADN</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Gènes fongiques</term><term>Milieux de culture</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report cloning and sequencing of gene ps1 encoding a versatile peroxidase combining catalytic properties of lignin peroxidase (LiP) and manganese peroxidase (MnP) isolated from lignocellulose cultures of the white-rot fungus Pleurotus eryngii. The gene contains 15 putative introns, and the deduced amino acid sequence consists of a 339-residue mature protein with a 31-residue signal peptide. Several putative response elements were identified in the promoter region. Amino acid residues involved in oxidation of Mn(2+) and aromatic substrates by direct electron transfer to heme and long-range electron transfer from superficial residues as predicted by analogy with Phanerochaete chrysosporium MnP and LiP, respectively. A dendrogram is presented illustrating sequence relationships between 29 fungal peroxidases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11004397</PMID><DateCompleted><Year>2000</Year><Month>12</Month><Day>01</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0378-1097</ISSN><JournalIssue CitedMedium="Print"><Volume>191</Volume><Issue>1</Issue><PubDate><Year>2000</Year><Month>Oct</Month><Day>01</Day></PubDate></JournalIssue><Title>FEMS microbiology letters</Title><ISOAbbreviation>FEMS Microbiol Lett</ISOAbbreviation></Journal><ArticleTitle>The cloning of a new peroxidase found in lignocellulose cultures of Pleurotus eryngii and sequence comparison with other fungal peroxidases.</ArticleTitle><Pagination><MedlinePgn>37-43</MedlinePgn></Pagination><Abstract><AbstractText>We report cloning and sequencing of gene ps1 encoding a versatile peroxidase combining catalytic properties of lignin peroxidase (LiP) and manganese peroxidase (MnP) isolated from lignocellulose cultures of the white-rot fungus Pleurotus eryngii. The gene contains 15 putative introns, and the deduced amino acid sequence consists of a 339-residue mature protein with a 31-residue signal peptide. Several putative response elements were identified in the promoter region. Amino acid residues involved in oxidation of Mn(2+) and aromatic substrates by direct electron transfer to heme and long-range electron transfer from superficial residues as predicted by analogy with Phanerochaete chrysosporium MnP and LiP, respectively. 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IdType="doi">10.1111/j.1574-6968.2000.tb09316.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Communauté de Madrid</li></region><settlement><li>Madrid</li></settlement></list><tree><noCountry><name sortKey="Martinez, A T" sort="Martinez, A T" uniqKey="Martinez A" first="A T" last="Martínez">A T Martínez</name><name sortKey="Martinez, M J" sort="Martinez, M J" uniqKey="Martinez M" first="M J" last="Martínez">M J Martínez</name><name sortKey="Ruiz Due As, F J" sort="Ruiz Due As, F J" uniqKey="Ruiz Due As F" first="F J" last="Ruiz-Due As">F J Ruiz-Due As</name><name sortKey="Sarkar, S" sort="Sarkar, S" uniqKey="Sarkar S" first="S" last="Sarkar">S. Sarkar</name></noCountry><country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Camarero, S" sort="Camarero, S" uniqKey="Camarero S" first="S" last="Camarero">S. Camarero</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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