Gene cloning and heterologous expression of glycoside hydrolase family 55 beta-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.
Identifieur interne : 000776 ( Main/Exploration ); précédent : 000775; suivant : 000777Gene cloning and heterologous expression of glycoside hydrolase family 55 beta-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.
Auteurs : Rie Kawai [Japon] ; Kiyohiko Igarashi ; Masahiro SamejimaSource :
- Biotechnology letters [ 0141-5492 ] ; 2006.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), Données de séquences moléculaires (MeSH), Glucan 1,3-beta-glucosidase (composition chimique), Glucan 1,3-beta-glucosidase (génétique), Glucan 1,3-beta-glucosidase (métabolisme), Glucanes (MeSH), Phanerochaete (enzymologie), Phanerochaete (génétique), Polyosides (métabolisme), Protéines recombinantes (biosynthèse), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- biosynthèse : Protéines recombinantes.
- composition chimique : Glucan 1,3-beta-glucosidase.
- enzymologie : Phanerochaete.
- génétique : ADN complémentaire, Glucan 1,3-beta-glucosidase, Phanerochaete.
- métabolisme : Glucan 1,3-beta-glucosidase, Polyosides.
- Données de séquences moléculaires, Glucanes, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), DNA, Complementary (genetics), Glucan 1,3-beta-Glucosidase (chemistry), Glucan 1,3-beta-Glucosidase (genetics), Glucan 1,3-beta-Glucosidase (metabolism), Glucans (MeSH), Molecular Sequence Data (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Polysaccharides (metabolism), Recombinant Proteins (biosynthesis), Substrate Specificity (MeSH).
- MESH :
- chemical , biosynthesis : Recombinant Proteins.
- chemical , chemistry : Glucan 1,3-beta-Glucosidase.
- chemical , genetics : DNA, Complementary, Glucan 1,3-beta-Glucosidase.
- chemical , metabolism : Glucan 1,3-beta-Glucosidase, Polysaccharides.
- enzymology : Phanerochaete.
- genetics : Phanerochaete.
- Amino Acid Sequence, Glucans, Molecular Sequence Data, Substrate Specificity.
Abstract
The basidiomycete Phanerochaete chrysosporium produces several beta-1,3-glucanases when grown on laminarin, a beta-1,3/1,6-glucan, as the sole carbon source. To characterize one of the major unknown beta-1, 3-glucanases with a molecular mass of 83 kDa, identification, cloning, and heterologous over-expression were carried out using the total genomic information of P. chrysosporium. The cDNA encoding this enzyme included an ORF of 2337 bp and the deduced amino acid sequence contains a predicted signal peptide of 26 amino acids and the mature protein of 752 amino acids. The amino acid sequence showed a significant similarity with glycoside hydrolase family 55 enzymes from filamentous fungi and was named Lam55A. Since the recombinant Lam55A expressed in the methylotrophic yeast Pichia pastoris degraded branched beta-1,3/1,6-glucan as well as linear beta-1,3-glucan, the kinetic features of the enzyme were compared with those of other beta-1,3-glucanases.
DOI: 10.1007/s10529-005-6179-7
PubMed: 16614901
Affiliations:
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To characterize one of the major unknown beta-1, 3-glucanases with a molecular mass of 83 kDa, identification, cloning, and heterologous over-expression were carried out using the total genomic information of P. chrysosporium. The cDNA encoding this enzyme included an ORF of 2337 bp and the deduced amino acid sequence contains a predicted signal peptide of 26 amino acids and the mature protein of 752 amino acids. The amino acid sequence showed a significant similarity with glycoside hydrolase family 55 enzymes from filamentous fungi and was named Lam55A. Since the recombinant Lam55A expressed in the methylotrophic yeast Pichia pastoris degraded branched beta-1,3/1,6-glucan as well as linear beta-1,3-glucan, the kinetic features of the enzyme were compared with those of other beta-1,3-glucanases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16614901</PMID><DateCompleted><Year>2006</Year><Month>07</Month><Day>28</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0141-5492</ISSN><JournalIssue CitedMedium="Print"><Volume>28</Volume><Issue>6</Issue><PubDate><Year>2006</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Biotechnology letters</Title><ISOAbbreviation>Biotechnol Lett</ISOAbbreviation></Journal><ArticleTitle>Gene cloning and heterologous expression of glycoside hydrolase family 55 beta-1,3-glucanase from the basidiomycete Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>365-71</MedlinePgn></Pagination><Abstract><AbstractText>The basidiomycete Phanerochaete chrysosporium produces several beta-1,3-glucanases when grown on laminarin, a beta-1,3/1,6-glucan, as the sole carbon source. To characterize one of the major unknown beta-1, 3-glucanases with a molecular mass of 83 kDa, identification, cloning, and heterologous over-expression were carried out using the total genomic information of P. chrysosporium. The cDNA encoding this enzyme included an ORF of 2337 bp and the deduced amino acid sequence contains a predicted signal peptide of 26 amino acids and the mature protein of 752 amino acids. The amino acid sequence showed a significant similarity with glycoside hydrolase family 55 enzymes from filamentous fungi and was named Lam55A. 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uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name></noCountry><country name="Japon"><region name="Région de Kantō"><name sortKey="Kawai, Rie" sort="Kawai, Rie" uniqKey="Kawai R" first="Rie" last="Kawai">Rie Kawai</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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