Molecular characterization of lignin peroxidase from the white-rot basidiomycete Trametes cervina: a novel fungal peroxidase.
Identifieur interne : 000550 ( Main/Exploration ); précédent : 000549; suivant : 000551Molecular characterization of lignin peroxidase from the white-rot basidiomycete Trametes cervina: a novel fungal peroxidase.
Auteurs : Yuta Miki [Japon] ; Hirofumi Ichinose ; Hiroyuki WariishiSource :
- FEMS microbiology letters [ 1574-6968 ] ; 2010.
Descripteurs français
- KwdFr :
- Analyse de séquence d'ADN (MeSH), Données de séquences moléculaires (MeSH), Modèles moléculaires (MeSH), Oxydoréduction (MeSH), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Séquence d'acides aminés (MeSH), Trametes (classification), Trametes (enzymologie), Trametes (génétique), Tryptophane (composition chimique), Tyrosine (composition chimique).
- MESH :
- composition chimique : Peroxidases, Protéines fongiques, Trametes, Tryptophane, Tyrosine.
- enzymologie : Trametes.
- génétique : Peroxidases, Protéines fongiques, Trametes.
- métabolisme : Peroxidases, Protéines fongiques.
- Analyse de séquence d'ADN, Données de séquences moléculaires, Modèles moléculaires, Oxydoréduction, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Sequence Analysis, DNA (MeSH), Trametes (classification), Trametes (enzymology), Trametes (genetics), Tryptophan (chemistry), Tyrosine (chemistry).
- MESH :
- chemical , chemistry : Fungal Proteins, Peroxidases, Tryptophan, Tyrosine.
- chemical , genetics : Fungal Proteins, Peroxidases.
- chemical , metabolism : Fungal Proteins, Peroxidases.
- classification : Trametes.
- enzymology : Trametes.
- genetics : Trametes.
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Oxidation-Reduction, Sequence Analysis, DNA.
Abstract
The lignin peroxidase (LiP) from Trametes cervina was cloned, characterized, and identified as a novel fungal peroxidase. The sequence of T. cervina LiP encodes the essential amino acids for shaping the heme cavity and calcium-binding sites, which are conserved in plant and fungal peroxidases. However, a sequence homology analysis showed that T. cervina LiP has two unique features: it lacks the conserved tryptophan residue corresponding to the substrate-oxidation site (Trp171) of Phanerochaete chrysosporium LiP and it has a tyrosine residue (Tyr181) that has never been reported in other lignin peroxidases. A tertiary model of T. cervina LiP showed that Tyr181 sterically adjacent to the 6-propionate group of heme is surrounded by acidic amino acids and is exposed to the exterior. These attributes indicate that Tyr181 could be a T. cervina LiP substrate-oxidation site. A phylogenetic analysis showed that T. cervina LiP does not cluster with any other fungal peroxidases, suggesting that it is a unique molecule that is evolutionarily distant from other peroxidases. Thus, we concluded that T. cervina LiP could be a novel secreted peroxidase, among those produced by fungi, with a new oxidation mechanism probably involving Tyr181.
DOI: 10.1111/j.1574-6968.2009.01880.x
PubMed: 20070371
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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The sequence of T. cervina LiP encodes the essential amino acids for shaping the heme cavity and calcium-binding sites, which are conserved in plant and fungal peroxidases. However, a sequence homology analysis showed that T. cervina LiP has two unique features: it lacks the conserved tryptophan residue corresponding to the substrate-oxidation site (Trp171) of Phanerochaete chrysosporium LiP and it has a tyrosine residue (Tyr181) that has never been reported in other lignin peroxidases. A tertiary model of T. cervina LiP showed that Tyr181 sterically adjacent to the 6-propionate group of heme is surrounded by acidic amino acids and is exposed to the exterior. These attributes indicate that Tyr181 could be a T. cervina LiP substrate-oxidation site. A phylogenetic analysis showed that T. cervina LiP does not cluster with any other fungal peroxidases, suggesting that it is a unique molecule that is evolutionarily distant from other peroxidases. Thus, we concluded that T. cervina LiP could be a novel secreted peroxidase, among those produced by fungi, with a new oxidation mechanism probably involving Tyr181.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20070371</PMID><DateCompleted><Year>2010</Year><Month>04</Month><Day>26</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1574-6968</ISSN><JournalIssue CitedMedium="Internet"><Volume>304</Volume><Issue>1</Issue><PubDate><Year>2010</Year><Month>Mar</Month></PubDate></JournalIssue><Title>FEMS microbiology letters</Title><ISOAbbreviation>FEMS Microbiol Lett</ISOAbbreviation></Journal><ArticleTitle>Molecular characterization of lignin peroxidase from the white-rot basidiomycete Trametes cervina: a novel fungal peroxidase.</ArticleTitle><Pagination><MedlinePgn>39-46</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.1574-6968.2009.01880.x</ELocationID><Abstract><AbstractText>The lignin peroxidase (LiP) from Trametes cervina was cloned, characterized, and identified as a novel fungal peroxidase. The sequence of T. cervina LiP encodes the essential amino acids for shaping the heme cavity and calcium-binding sites, which are conserved in plant and fungal peroxidases. However, a sequence homology analysis showed that T. cervina LiP has two unique features: it lacks the conserved tryptophan residue corresponding to the substrate-oxidation site (Trp171) of Phanerochaete chrysosporium LiP and it has a tyrosine residue (Tyr181) that has never been reported in other lignin peroxidases. A tertiary model of T. cervina LiP showed that Tyr181 sterically adjacent to the 6-propionate group of heme is surrounded by acidic amino acids and is exposed to the exterior. These attributes indicate that Tyr181 could be a T. cervina LiP substrate-oxidation site. A phylogenetic analysis showed that T. cervina LiP does not cluster with any other fungal peroxidases, suggesting that it is a unique molecule that is evolutionarily distant from other peroxidases. 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PubStatus="pubmed"><Year>2010</Year><Month>1</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>4</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20070371</ArticleId><ArticleId IdType="pii">FML1880</ArticleId><ArticleId IdType="doi">10.1111/j.1574-6968.2009.01880.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Kyūshū</li><li>Préfecture de Fukuoka</li></region><settlement><li>Fukuoka</li></settlement><orgName><li>Université de Kyūshū</li></orgName></list><tree><noCountry><name sortKey="Ichinose, Hirofumi" sort="Ichinose, Hirofumi" uniqKey="Ichinose H" first="Hirofumi" last="Ichinose">Hirofumi Ichinose</name><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name></noCountry><country name="Japon"><region name="Kyūshū"><name sortKey="Miki, Yuta" sort="Miki, Yuta" uniqKey="Miki Y" first="Yuta" last="Miki">Yuta Miki</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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