Characterization of an endoglucanase belonging to a new subfamily of glycoside hydrolase family 45 of the basidiomycete Phanerochaete chrysosporium.
Identifieur interne : 000673 ( Main/Curation ); précédent : 000672; suivant : 000674Characterization of an endoglucanase belonging to a new subfamily of glycoside hydrolase family 45 of the basidiomycete Phanerochaete chrysosporium.
Auteurs : Kiyohiko Igarashi [Japon] ; Takuya Ishida ; Chiaki Hori ; Masahiro SamejimaSource :
- Applied and environmental microbiology [ 1098-5336 ] ; 2008.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), ADN fongique (génétique), Alignement de séquences (MeSH), Cellulase (génétique), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Expression des gènes (MeSH), Glycosidases (génétique), Gènes fongiques (MeSH), Phanerochaete (enzymologie), Phanerochaete (génétique), Phylogenèse (MeSH), Protéines fongiques (génétique), Protéines recombinantes (génétique), RT-PCR (MeSH), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- enzymologie : Phanerochaete.
- génétique : ADN complémentaire, ADN fongique, Cellulase, Glycosidases, Phanerochaete, Protéines fongiques, Protéines recombinantes.
- Alignement de séquences, Clonage moléculaire, Données de séquences moléculaires, Expression des gènes, Gènes fongiques, Phylogenèse, RT-PCR, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Cellulase (genetics), Cloning, Molecular (MeSH), DNA, Complementary (genetics), DNA, Fungal (genetics), Fungal Proteins (genetics), Gene Expression (MeSH), Genes, Fungal (MeSH), Glycoside Hydrolases (genetics), Molecular Sequence Data (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Phylogeny (MeSH), Recombinant Proteins (genetics), Reverse Transcriptase Polymerase Chain Reaction (MeSH), Sequence Alignment (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , genetics : Cellulase, DNA, Complementary, DNA, Fungal, Fungal Proteins, Glycoside Hydrolases, Recombinant Proteins.
- enzymology : Phanerochaete.
- genetics : Phanerochaete.
- Amino Acid Sequence, Cloning, Molecular, Gene Expression, Genes, Fungal, Molecular Sequence Data, Phylogeny, Reverse Transcriptase Polymerase Chain Reaction, Sequence Alignment, Substrate Specificity.
Abstract
The wood decay fungus Phanerochaete chrysosporium has served as a model system for the study of lignocellulose conversions, but aspects of its cellulolytic system remain uncertain. Here, we report identifying the gene that encodes the glycoside hydrolase (GH) family 45 endoglucanase (EG) from the fungus, cloning the cDNA, determining its heterologous expression in the methylotrophic yeast Pichia pastoris, and characterizing the recombinant protein. The cDNA consisted of 718 bp, including an open reading frame encoding a 19-amino-acid signal peptide, a 7-amino-acid presequence at the N-terminal region, and a 180-amino-acid mature protein, which has no cellulose binding domain. Analysis of the amino acid sequence revealed that the protein has a low similarity (<22%) to known fungal EGs belonging to the GH family 45 (EGVs). No conserved domain of this family was found by a BLAST search, suggesting that the protein should be classified into a new subdivision of this GH family. The recombinant protein has hydrolytic activity toward amorphous cellulose, carboxylmethyl cellulose, lichenan, barley beta-glucan, and glucomannan but not xylan. Moreover, a synergistic effect was observed with the recombinant GH family 6 cellobiohydrolase from the same fungus toward amorphous cellulose as a substrate, indicating that the enzyme may act in concert with other cellulolytic enzymes to hydrolyze cellulosic biomass in nature.
DOI: 10.1128/AEM.00812-08
PubMed: 18676702
PubMed Central: PMC2547050
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Here, we report identifying the gene that encodes the glycoside hydrolase (GH) family 45 endoglucanase (EG) from the fungus, cloning the cDNA, determining its heterologous expression in the methylotrophic yeast Pichia pastoris, and characterizing the recombinant protein. The cDNA consisted of 718 bp, including an open reading frame encoding a 19-amino-acid signal peptide, a 7-amino-acid presequence at the N-terminal region, and a 180-amino-acid mature protein, which has no cellulose binding domain. Analysis of the amino acid sequence revealed that the protein has a low similarity (<22%) to known fungal EGs belonging to the GH family 45 (EGVs). No conserved domain of this family was found by a BLAST search, suggesting that the protein should be classified into a new subdivision of this GH family. The recombinant protein has hydrolytic activity toward amorphous cellulose, carboxylmethyl cellulose, lichenan, barley beta-glucan, and glucomannan but not xylan. Moreover, a synergistic effect was observed with the recombinant GH family 6 cellobiohydrolase from the same fungus toward amorphous cellulose as a substrate, indicating that the enzyme may act in concert with other cellulolytic enzymes to hydrolyze cellulosic biomass in nature.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18676702</PMID><DateCompleted><Year>2008</Year><Month>09</Month><Day>30</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5336</ISSN><JournalIssue CitedMedium="Internet"><Volume>74</Volume><Issue>18</Issue><PubDate><Year>2008</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>Characterization of an endoglucanase belonging to a new subfamily of glycoside hydrolase family 45 of the basidiomycete Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>5628-34</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/AEM.00812-08</ELocationID><Abstract><AbstractText>The wood decay fungus Phanerochaete chrysosporium has served as a model system for the study of lignocellulose conversions, but aspects of its cellulolytic system remain uncertain. Here, we report identifying the gene that encodes the glycoside hydrolase (GH) family 45 endoglucanase (EG) from the fungus, cloning the cDNA, determining its heterologous expression in the methylotrophic yeast Pichia pastoris, and characterizing the recombinant protein. The cDNA consisted of 718 bp, including an open reading frame encoding a 19-amino-acid signal peptide, a 7-amino-acid presequence at the N-terminal region, and a 180-amino-acid mature protein, which has no cellulose binding domain. Analysis of the amino acid sequence revealed that the protein has a low similarity (<22%) to known fungal EGs belonging to the GH family 45 (EGVs). No conserved domain of this family was found by a BLAST search, suggesting that the protein should be classified into a new subdivision of this GH family. The recombinant protein has hydrolytic activity toward amorphous cellulose, carboxylmethyl cellulose, lichenan, barley beta-glucan, and glucomannan but not xylan. 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|texte= Characterization of an endoglucanase belonging to a new subfamily of glycoside hydrolase family 45 of the basidiomycete Phanerochaete chrysosporium.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Curation/RBID.i -Sk "pubmed:18676702" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Curation/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |