Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii.
Identifieur interne : 000B18 ( Main/Exploration ); précédent : 000B17; suivant : 000B19Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii.
Auteurs : F J Ruiz-Due As [Espagne] ; M J Martínez ; A T MartínezSource :
- Molecular microbiology [ 0950-382X ] ; 1999.
Descripteurs français
- KwdFr :
- ADN fongique (MeSH), Analyse de séquence (MeSH), Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Isoenzymes (composition chimique), Isoenzymes (génétique), Isoenzymes (métabolisme), Manganèse (MeSH), Modèles moléculaires (MeSH), Myeloperoxidase (composition chimique), Myeloperoxidase (génétique), Myeloperoxidase (métabolisme), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Pleurotus (enzymologie), Pleurotus (génétique), Protéines fongiques (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Isoenzymes, Myeloperoxidase, Peroxidases.
- enzymologie : Pleurotus.
- génétique : Isoenzymes, Myeloperoxidase, Peroxidases, Pleurotus.
- métabolisme : Isoenzymes, Myeloperoxidase, Peroxidases.
- ADN fongique, Analyse de séquence, Clonage moléculaire, Conformation des protéines, Données de séquences moléculaires, Manganèse, Modèles moléculaires, Protéines fongiques, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), DNA, Fungal (MeSH), Fungal Proteins (MeSH), Isoenzymes (chemistry), Isoenzymes (genetics), Isoenzymes (metabolism), Manganese (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Peroxidase (chemistry), Peroxidase (genetics), Peroxidase (metabolism), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Pleurotus (enzymology), Pleurotus (genetics), Protein Conformation (MeSH), Sequence Analysis (MeSH).
- MESH :
- chemical , chemistry : Isoenzymes, Peroxidase, Peroxidases.
- chemical , genetics : Isoenzymes, Peroxidase, Peroxidases.
- chemical , metabolism : Isoenzymes, Peroxidase, Peroxidases.
- chemical : DNA, Fungal, Fungal Proteins, Manganese.
- enzymology : Pleurotus.
- genetics : Pleurotus.
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Analysis.
Abstract
A haem peroxidase different from other microbial, plant and animal peroxidases is described. The enzyme is secreted as two isoforms by dikaryotic Pleurotus eryngii in peptone-containing liquid medium. The corresponding gene, which presents 15 introns and encodes a 361-amino-acid protein with a 30-amino-acid signal peptide, was isolated as two alleles corresponding to the two isoforms. The alleles differ in three amino acid residues and in a seven nucleotide deletion affecting a single metal response element in the promoter. When compared with Phanerochaete chrysosporium peroxidases, the new enzyme appears closer to lignin peroxidase (LiP) than to Mn-dependent peroxidase (MnP) isoenzymes (58-60% and 55% identity respectively). The molecular model built using crystal structures of three fungal peroxidases as templates, also showed high structural affinity with LiP (C alpha-distance 1.2 A). However, this peroxidase includes a Mn2+ binding site formed by three acidic residues (E36, E40 and D175) near the haem internal propionate, which accounts for the ability to oxidize Mn2+. Its capability to oxidize aromatic substrates could involve interactions with aromatic residues at the edge of the haem channel. Another possibility is long-range electron transfer, e.g. from W164, which occupies the same position of LiP W171 recently reported as involved in the catalytic cycle of LiP.
DOI: 10.1046/j.1365-2958.1999.01164.x
PubMed: 9987124
Affiliations:
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The enzyme is secreted as two isoforms by dikaryotic Pleurotus eryngii in peptone-containing liquid medium. The corresponding gene, which presents 15 introns and encodes a 361-amino-acid protein with a 30-amino-acid signal peptide, was isolated as two alleles corresponding to the two isoforms. The alleles differ in three amino acid residues and in a seven nucleotide deletion affecting a single metal response element in the promoter. When compared with Phanerochaete chrysosporium peroxidases, the new enzyme appears closer to lignin peroxidase (LiP) than to Mn-dependent peroxidase (MnP) isoenzymes (58-60% and 55% identity respectively). The molecular model built using crystal structures of three fungal peroxidases as templates, also showed high structural affinity with LiP (C alpha-distance 1.2 A). However, this peroxidase includes a Mn2+ binding site formed by three acidic residues (E36, E40 and D175) near the haem internal propionate, which accounts for the ability to oxidize Mn2+. Its capability to oxidize aromatic substrates could involve interactions with aromatic residues at the edge of the haem channel. 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The enzyme is secreted as two isoforms by dikaryotic Pleurotus eryngii in peptone-containing liquid medium. The corresponding gene, which presents 15 introns and encodes a 361-amino-acid protein with a 30-amino-acid signal peptide, was isolated as two alleles corresponding to the two isoforms. The alleles differ in three amino acid residues and in a seven nucleotide deletion affecting a single metal response element in the promoter. When compared with Phanerochaete chrysosporium peroxidases, the new enzyme appears closer to lignin peroxidase (LiP) than to Mn-dependent peroxidase (MnP) isoenzymes (58-60% and 55% identity respectively). The molecular model built using crystal structures of three fungal peroxidases as templates, also showed high structural affinity with LiP (C alpha-distance 1.2 A). However, this peroxidase includes a Mn2+ binding site formed by three acidic residues (E36, E40 and D175) near the haem internal propionate, which accounts for the ability to oxidize Mn2+. Its capability to oxidize aromatic substrates could involve interactions with aromatic residues at the edge of the haem channel. 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PubStatus="pubmed"><Year>1999</Year><Month>2</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>2</Month><Day>13</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>2</Month><Day>13</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">9987124</ArticleId><ArticleId IdType="doi">10.1046/j.1365-2958.1999.01164.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></noCountry><country name="Espagne"><region name="Communauté de Madrid"><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></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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