Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1.
Identifieur interne : 000B95 ( Main/Exploration ); précédent : 000B94; suivant : 000B96Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1.
Auteurs : G. Henriksson [Suède] ; A. Salumets ; C. Divne ; G. PetterssonSource :
- The Biochemical journal [ 0264-6021 ] ; 1997.
Descripteurs français
- KwdFr :
- Basidiomycota (enzymologie), Carbohydrate dehydrogenases (métabolisme), Cellulase (métabolisme), Cellulose (métabolisme), Cellulose 1,4-beta-cellobiosidase (MeSH), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Liaison aux protéines (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Carbohydrate Dehydrogenases, Cellulase, Cellulose.
- enzymology : Basidiomycota.
- Amino Acid Sequence, Cellulose 1,4-beta-Cellobiosidase, Kinetics, Molecular Sequence Data, Protein Binding, Sequence Homology, Amino Acid.
Abstract
The binding isotherm to cellulose of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium has been compared with that of cellobiohydrolase 1 (CBH 1) from Trichoderma reesei. CDH binds more strongly but more sparsely to cellulose than does CBH 1. In a classical Scatchard analysis, a better fit to a one-site binding model was obtained for CDH than for CBH 1. The binding of both enzymes decreased in the presence of ethylene glycol, increased in the presence of ammonium sulphate and was unaffected by sodium chloride. Attempts to localize the cellulose-binding site on CDH have also been made by exposing enzymically digested CDH to cellulose and isolating the cellulose-bound peptides. The results suggest that the cellulose-binding site is located internally in the amino acid sequence of CDH.
DOI: 10.1042/bj3240833
PubMed: 9210407
PubMed Central: PMC1218499
Affiliations:
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Pettersson</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="ISSN">0264-6021</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Basidiomycota (enzymology)</term><term>Carbohydrate Dehydrogenases (metabolism)</term><term>Cellulase (metabolism)</term><term>Cellulose (metabolism)</term><term>Cellulose 1,4-beta-Cellobiosidase (MeSH)</term><term>Kinetics (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Protein Binding (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Basidiomycota (enzymologie)</term><term>Carbohydrate dehydrogenases (métabolisme)</term><term>Cellulase (métabolisme)</term><term>Cellulose (métabolisme)</term><term>Cellulose 1,4-beta-cellobiosidase (MeSH)</term><term>Cinétique (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbohydrate Dehydrogenases</term><term>Cellulase</term><term>Cellulose</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Basidiomycota</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carbohydrate dehydrogenases</term><term>Cellulase</term><term>Cellulose</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cellulose 1,4-beta-Cellobiosidase</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellulose 1,4-beta-cellobiosidase</term><term>Cinétique</term><term>Données de séquences moléculaires</term><term>Liaison aux protéines</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The binding isotherm to cellulose of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium has been compared with that of cellobiohydrolase 1 (CBH 1) from Trichoderma reesei. CDH binds more strongly but more sparsely to cellulose than does CBH 1. In a classical Scatchard analysis, a better fit to a one-site binding model was obtained for CDH than for CBH 1. The binding of both enzymes decreased in the presence of ethylene glycol, increased in the presence of ammonium sulphate and was unaffected by sodium chloride. Attempts to localize the cellulose-binding site on CDH have also been made by exposing enzymically digested CDH to cellulose and isolating the cellulose-bound peptides. The results suggest that the cellulose-binding site is located internally in the amino acid sequence of CDH.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9210407</PMID><DateCompleted><Year>1997</Year><Month>07</Month><Day>28</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0264-6021</ISSN><JournalIssue CitedMedium="Print"><Volume>324 ( Pt 3)</Volume><PubDate><Year>1997</Year><Month>Jun</Month><Day>15</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Studies of cellulose binding by cellobiose dehydrogenase and a comparison with cellobiohydrolase 1.</ArticleTitle><Pagination><MedlinePgn>833-8</MedlinePgn></Pagination><Abstract><AbstractText>The binding isotherm to cellulose of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium has been compared with that of cellobiohydrolase 1 (CBH 1) from Trichoderma reesei. CDH binds more strongly but more sparsely to cellulose than does CBH 1. In a classical Scatchard analysis, a better fit to a one-site binding model was obtained for CDH than for CBH 1. The binding of both enzymes decreased in the presence of ethylene glycol, increased in the presence of ammonium sulphate and was unaffected by sodium chloride. Attempts to localize the cellulose-binding site on CDH have also been made by exposing enzymically digested CDH to cellulose and isolating the cellulose-bound peptides. The results suggest that the cellulose-binding site is located internally in the amino acid sequence of CDH.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Henriksson</LastName><ForeName>G</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Uppsala, Biomedical Center, Box 576, S-751 23 Uppsala, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Salumets</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Divne</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Pettersson</LastName><ForeName>G</ForeName><Initials>G</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. 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Divne</name><name sortKey="Pettersson, G" sort="Pettersson, G" uniqKey="Pettersson G" first="G" last="Pettersson">G. Pettersson</name><name sortKey="Salumets, A" sort="Salumets, A" uniqKey="Salumets A" first="A" last="Salumets">A. Salumets</name></noCountry><country name="Suède"><noRegion><name sortKey="Henriksson, G" sort="Henriksson, G" uniqKey="Henriksson G" first="G" last="Henriksson">G. Henriksson</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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