PhanerochaeteV1, Main, Exploration, bibRecord, 000F95

Cellulase families revealed by hydrophobic cluster analysis.

Identifieur interne : 000F95 ( Main/Exploration ); précédent : 000F94; suivant : 000F96

Cellulase families revealed by hydrophobic cluster analysis.

Auteurs : B. Henrissat [France] ; M. Claeyssens ; P. Tomme ; L. Lemesle ; J P Mornon

Source :

Gene [ 0378-1119 ] ; 1989.

RBID : pubmed:2806912

Descripteurs français

KwdFr :
- Analyse de regroupements (MeSH), Bactéries (enzymologie), Bactéries (génétique), Cellulase (classification), Cellulase (génétique), Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Similitude de séquences d'acides nucléiques (MeSH), Sites de fixation (MeSH), Solubilité (MeSH), Séquence d'acides aminés (MeSH).
MESH :
- classification : Cellulase.
- enzymologie : Bactéries.
- génétique : Bactéries, Cellulase.
- Analyse de regroupements, Conformation des protéines, Données de séquences moléculaires, Similitude de séquences d'acides nucléiques, Sites de fixation, Solubilité, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Bacteria (enzymology), Bacteria (genetics), Binding Sites (MeSH), Cellulase (classification), Cellulase (genetics), Cluster Analysis (MeSH), Molecular Sequence Data (MeSH), Protein Conformation (MeSH), Sequence Homology, Nucleic Acid (MeSH), Solubility (MeSH).
MESH :
- chemical , classification : Cellulase.
- enzymology : Bacteria.
- genetics : Bacteria, Cellulase.
- Amino Acid Sequence, Binding Sites, Cluster Analysis, Molecular Sequence Data, Protein Conformation, Sequence Homology, Nucleic Acid, Solubility.

Abstract

The amino acid sequences of 21 beta-glycanases have been compared by hydrophobic cluster analysis. Six families of cellulases have been identified on the basis of primary structure homology: (A) endoglucanases B, C and E of Clostridium thermocellum; endoglucanases of Erwinia chrysanthemi and Bacillus sp.; endoglucanase III of Trichoderma reesei; endoglucanase I of Schizophyllum commune; (B) cellobiohydrolase II of T. reesei; endoglucanases of Cellulomonas fimi and Streptomyces sp; (C) cellobiohydrolases I of T. reesei and of Phanerochaete chrysosporium; endoglucanase I of T. reesei; (D) endoglucanase A of C. thermocellum and an endoglucanase from Ce. uda; (E) endoglucanase D of C. thermocellum and an endoglucanase from Pseudomonas fluorescens; (F) xylanases of C. thermocellum and of Cryptococcus albidus and the cellobio-hydrolase of Ce. fimi. For each family, conserved potentially catalytic residues have have been listed and previous allocations of the active-site residues are evaluated in the light of the alignment of the amino acid sequences. A strong homology is also reported for the putative cellulose-binding domains of cellulases of Ce. fimi and of P. fluorescens.

DOI: 10.1016/0378-1119(89)90339-9
PubMed: 2806912

Affiliations:

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Le document en format XML

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<term>Bacteria (enzymology)</term>
<term>Bacteria (genetics)</term>
<term>Binding Sites (MeSH)</term>
<term>Cellulase (classification)</term>
<term>Cellulase (genetics)</term>
<term>Cluster Analysis (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Protein Conformation (MeSH)</term>
<term>Sequence Homology, Nucleic Acid (MeSH)</term>
<term>Solubility (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de regroupements (MeSH)</term>
<term>Bactéries (enzymologie)</term>
<term>Bactéries (génétique)</term>
<term>Cellulase (classification)</term>
<term>Cellulase (génétique)</term>
<term>Conformation des protéines (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Similitude de séquences d'acides nucléiques (MeSH)</term>
<term>Sites de fixation (MeSH)</term>
<term>Solubilité (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Cellulase</term>
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<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Bactéries</term>
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<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bacteria</term>
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<term>Cellulase</term>
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<term>Cellulase</term>
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<term>Binding Sites</term>
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<term>Protein Conformation</term>
<term>Sequence Homology, Nucleic Acid</term>
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<term>Données de séquences moléculaires</term>
<term>Similitude de séquences d'acides nucléiques</term>
<term>Sites de fixation</term>
<term>Solubilité</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">The amino acid sequences of 21 beta-glycanases have been compared by hydrophobic cluster analysis. Six families of cellulases have been identified on the basis of primary structure homology: (A) endoglucanases B, C and E of Clostridium thermocellum; endoglucanases of Erwinia chrysanthemi and Bacillus sp.; endoglucanase III of Trichoderma reesei; endoglucanase I of Schizophyllum commune; (B) cellobiohydrolase II of T. reesei; endoglucanases of Cellulomonas fimi and Streptomyces sp; (C) cellobiohydrolases I of T. reesei and of Phanerochaete chrysosporium; endoglucanase I of T. reesei; (D) endoglucanase A of C. thermocellum and an endoglucanase from Ce. uda; (E) endoglucanase D of C. thermocellum and an endoglucanase from Pseudomonas fluorescens; (F) xylanases of C. thermocellum and of Cryptococcus albidus and the cellobio-hydrolase of Ce. fimi. For each family, conserved potentially catalytic residues have have been listed and previous allocations of the active-site residues are evaluated in the light of the alignment of the amino acid sequences. A strong homology is also reported for the putative cellulose-binding domains of cellulases of Ce. fimi and of P. fluorescens.</div>
</front>
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<Title>Gene</Title>
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<Abstract><AbstractText>The amino acid sequences of 21 beta-glycanases have been compared by hydrophobic cluster analysis. Six families of cellulases have been identified on the basis of primary structure homology: (A) endoglucanases B, C and E of Clostridium thermocellum; endoglucanases of Erwinia chrysanthemi and Bacillus sp.; endoglucanase III of Trichoderma reesei; endoglucanase I of Schizophyllum commune; (B) cellobiohydrolase II of T. reesei; endoglucanases of Cellulomonas fimi and Streptomyces sp; (C) cellobiohydrolases I of T. reesei and of Phanerochaete chrysosporium; endoglucanase I of T. reesei; (D) endoglucanase A of C. thermocellum and an endoglucanase from Ce. uda; (E) endoglucanase D of C. thermocellum and an endoglucanase from Pseudomonas fluorescens; (F) xylanases of C. thermocellum and of Cryptococcus albidus and the cellobio-hydrolase of Ce. fimi. For each family, conserved potentially catalytic residues have have been listed and previous allocations of the active-site residues are evaluated in the light of the alignment of the amino acid sequences. A strong homology is also reported for the putative cellulose-binding domains of cellulases of Ce. fimi and of P. fluorescens.</AbstractText>
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Cellulase families revealed by hydrophobic cluster analysis.

Cellulase families revealed by hydrophobic cluster analysis.

Source :

Descripteurs français

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki