Characterization of a novel PQQ-dependent quinohemoprotein pyranose dehydrogenase from Coprinopsis cinerea classified into auxiliary activities family 12 in carbohydrate-active enzymes.
Identifieur interne : 000274 ( Main/Exploration ); précédent : 000273; suivant : 000275Characterization of a novel PQQ-dependent quinohemoprotein pyranose dehydrogenase from Coprinopsis cinerea classified into auxiliary activities family 12 in carbohydrate-active enzymes.
Auteurs : Kouta Takeda [Japon] ; Hirotoshi Matsumura [Japon] ; Takuya Ishida [Japon] ; Masahiro Samejima [Japon] ; Hiroyuki Ohno [Japon] ; Makoto Yoshida [Japon] ; Kiyohiko Igarashi [Japon] ; Nobuhumi Nakamura [Japon]Source :
- PloS one [ 1932-6203 ] ; 2015.
Descripteurs français
- KwdFr :
- Agaricales (enzymologie), Animaux (MeSH), Biocatalyse (MeSH), Cofacteur PQQ (métabolisme), Données de séquences moléculaires (MeSH), Métabolisme glucidique (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Électrochimie (MeSH).
- MESH :
- composition chimique : Oxidoreductases.
- enzymologie : Agaricales.
- métabolisme : Cofacteur PQQ, Oxidoreductases.
- Animaux, Biocatalyse, Données de séquences moléculaires, Métabolisme glucidique, Structure tertiaire des protéines, Séquence d'acides aminés, Électrochimie.
English descriptors
- KwdEn :
- Agaricales (enzymology), Amino Acid Sequence (MeSH), Animals (MeSH), Biocatalysis (MeSH), Carbohydrate Metabolism (MeSH), Electrochemistry (MeSH), Molecular Sequence Data (MeSH), Oxidoreductases (chemistry), Oxidoreductases (metabolism), PQQ Cofactor (metabolism), Protein Structure, Tertiary (MeSH).
- MESH :
- chemical , chemistry : Oxidoreductases.
- enzymology : Agaricales.
- chemical , metabolism : Oxidoreductases, PQQ Cofactor.
- Amino Acid Sequence, Animals, Biocatalysis, Carbohydrate Metabolism, Electrochemistry, Molecular Sequence Data, Protein Structure, Tertiary.
Abstract
The basidiomycete Coprinopsis cinerea contains a quinohemoprotein (CcPDH named as CcSDH in our previous paper), which is a new type of pyrroloquinoline-quinone (PQQ)-dependent pyranose dehydrogenase and is the first found among all eukaryotes. This enzyme has a three-domain structure consisting of an N-terminal heme b containing a cytochrome domain that is homologous to the cytochrome domain of cellobiose dehydrogenase (CDH; EC 1.1.99.18) from the wood-rotting basidiomycete Phanerochaete chrysosporium, a C-terminal family 1-type carbohydrate-binding module, and a novel central catalytic domain containing PQQ as a cofactor. Here, we describe the biochemical and electrochemical characterization of recombinant CcPDH. UV-vis and resonance Raman spectroscopic studies clearly reveal characteristics of a 6-coordinated low-spin heme b in both the ferric and ferrous states, as well as intramolecular electron transfer from the PQQ to heme b. Moreover, the formal potential of the heme was evaluated to be 130 mV vs. NHE by cyclic voltammetry. These results indicate that the cytochrome domain of CcPDH possesses similar biophysical properties to that in CDH. A comparison of the conformations of monosaccharides as substrates and the associated catalytic efficiency (kcat/Km) of CcPDH indicates that the enzyme prefers monosaccharides with equatorial C-2, C-3 hydroxyl groups and an axial C-4 hydroxyl group in the 1C4 chair conformation. Furthermore, a binding study shows a high binding affinity of CcPDH for cellulose, suggesting that CcPDH function is related to the enzymatic degradation of plant cell wall.
DOI: 10.1371/journal.pone.0115722
PubMed: 25679509
PubMed Central: PMC4332668
Affiliations:
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Tokyo</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Matsumura, Hirotoshi" sort="Matsumura, Hirotoshi" uniqKey="Matsumura H" first="Hirotoshi" last="Matsumura">Hirotoshi Matsumura</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName><orgName type="university">Université de Tokyo</orgName></affiliation></author><author><name sortKey="Ishida, Takuya" sort="Ishida, Takuya" uniqKey="Ishida T" first="Takuya" last="Ishida">Takuya Ishida</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName><orgName type="university">Université de Tokyo</orgName></affiliation></author><author><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of 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first="Makoto" last="Yoshida">Makoto Yoshida</name><affiliation wicri:level="3"><nlm:affiliation>Department of Environmental and Natural Resource Science, Tokyo University of Agriculture and Technology, Tokyo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Environmental and Natural Resource Science, Tokyo University of Agriculture and Technology, Tokyo</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Igarashi, Kiyohiko" sort="Igarashi, Kiyohiko" uniqKey="Igarashi K" first="Kiyohiko" last="Igarashi">Kiyohiko Igarashi</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName><orgName type="university">Université de Tokyo</orgName></affiliation></author><author><name sortKey="Nakamura, Nobuhumi" sort="Nakamura, Nobuhumi" uniqKey="Nakamura N" first="Nobuhumi" last="Nakamura">Nobuhumi Nakamura</name><affiliation wicri:level="3"><nlm:affiliation>Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Agaricales (enzymology)</term><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Biocatalysis (MeSH)</term><term>Carbohydrate Metabolism (MeSH)</term><term>Electrochemistry (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidoreductases (chemistry)</term><term>Oxidoreductases (metabolism)</term><term>PQQ Cofactor (metabolism)</term><term>Protein Structure, Tertiary (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Agaricales (enzymologie)</term><term>Animaux (MeSH)</term><term>Biocatalyse (MeSH)</term><term>Cofacteur PQQ (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Métabolisme glucidique (MeSH)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (métabolisme)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Électrochimie (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Agaricales</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Agaricales</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases</term><term>PQQ Cofactor</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cofacteur PQQ</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Biocatalysis</term><term>Carbohydrate Metabolism</term><term>Electrochemistry</term><term>Molecular Sequence Data</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Biocatalyse</term><term>Données de séquences moléculaires</term><term>Métabolisme glucidique</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Électrochimie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The basidiomycete Coprinopsis cinerea contains a quinohemoprotein (CcPDH named as CcSDH in our previous paper), which is a new type of pyrroloquinoline-quinone (PQQ)-dependent pyranose dehydrogenase and is the first found among all eukaryotes. This enzyme has a three-domain structure consisting of an N-terminal heme b containing a cytochrome domain that is homologous to the cytochrome domain of cellobiose dehydrogenase (CDH; EC 1.1.99.18) from the wood-rotting basidiomycete Phanerochaete chrysosporium, a C-terminal family 1-type carbohydrate-binding module, and a novel central catalytic domain containing PQQ as a cofactor. Here, we describe the biochemical and electrochemical characterization of recombinant CcPDH. UV-vis and resonance Raman spectroscopic studies clearly reveal characteristics of a 6-coordinated low-spin heme b in both the ferric and ferrous states, as well as intramolecular electron transfer from the PQQ to heme b. Moreover, the formal potential of the heme was evaluated to be 130 mV vs. NHE by cyclic voltammetry. These results indicate that the cytochrome domain of CcPDH possesses similar biophysical properties to that in CDH. A comparison of the conformations of monosaccharides as substrates and the associated catalytic efficiency (kcat/Km) of CcPDH indicates that the enzyme prefers monosaccharides with equatorial C-2, C-3 hydroxyl groups and an axial C-4 hydroxyl group in the 1C4 chair conformation. Furthermore, a binding study shows a high binding affinity of CcPDH for cellulose, suggesting that CcPDH function is related to the enzymatic degradation of plant cell wall. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25679509</PMID><DateCompleted><Year>2016</Year><Month>01</Month><Day>13</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>10</Volume><Issue>2</Issue><PubDate><Year>2015</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Characterization of a novel PQQ-dependent quinohemoprotein pyranose dehydrogenase from Coprinopsis cinerea classified into auxiliary activities family 12 in carbohydrate-active enzymes.</ArticleTitle><Pagination><MedlinePgn>e0115722</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0115722</ELocationID><Abstract><AbstractText>The basidiomycete Coprinopsis cinerea contains a quinohemoprotein (CcPDH named as CcSDH in our previous paper), which is a new type of pyrroloquinoline-quinone (PQQ)-dependent pyranose dehydrogenase and is the first found among all eukaryotes. This enzyme has a three-domain structure consisting of an N-terminal heme b containing a cytochrome domain that is homologous to the cytochrome domain of cellobiose dehydrogenase (CDH; EC 1.1.99.18) from the wood-rotting basidiomycete Phanerochaete chrysosporium, a C-terminal family 1-type carbohydrate-binding module, and a novel central catalytic domain containing PQQ as a cofactor. Here, we describe the biochemical and electrochemical characterization of recombinant CcPDH. UV-vis and resonance Raman spectroscopic studies clearly reveal characteristics of a 6-coordinated low-spin heme b in both the ferric and ferrous states, as well as intramolecular electron transfer from the PQQ to heme b. Moreover, the formal potential of the heme was evaluated to be 130 mV vs. NHE by cyclic voltammetry. These results indicate that the cytochrome domain of CcPDH possesses similar biophysical properties to that in CDH. A comparison of the conformations of monosaccharides as substrates and the associated catalytic efficiency (kcat/Km) of CcPDH indicates that the enzyme prefers monosaccharides with equatorial C-2, C-3 hydroxyl groups and an axial C-4 hydroxyl group in the 1C4 chair conformation. Furthermore, a binding study shows a high binding affinity of CcPDH for cellulose, suggesting that CcPDH function is related to the enzymatic degradation of plant cell wall. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Takeda</LastName><ForeName>Kouta</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matsumura</LastName><ForeName>Hirotoshi</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ishida</LastName><ForeName>Takuya</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Samejima</LastName><ForeName>Masahiro</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ohno</LastName><ForeName>Hiroyuki</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yoshida</LastName><ForeName>Makoto</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Environmental and Natural Resource Science, Tokyo University of Agriculture and Technology, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Igarashi</LastName><ForeName>Kiyohiko</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biomaterials Sciences, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Tokyo, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>Nobuhumi</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>02</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS 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Hirotoshi" uniqKey="Matsumura H" first="Hirotoshi" last="Matsumura">Hirotoshi Matsumura</name><name sortKey="Nakamura, Nobuhumi" sort="Nakamura, Nobuhumi" uniqKey="Nakamura N" first="Nobuhumi" last="Nakamura">Nobuhumi Nakamura</name><name sortKey="Ohno, Hiroyuki" sort="Ohno, Hiroyuki" uniqKey="Ohno H" first="Hiroyuki" last="Ohno">Hiroyuki Ohno</name><name sortKey="Samejima, Masahiro" sort="Samejima, Masahiro" uniqKey="Samejima M" first="Masahiro" last="Samejima">Masahiro Samejima</name><name sortKey="Yoshida, Makoto" sort="Yoshida, Makoto" uniqKey="Yoshida M" first="Makoto" last="Yoshida">Makoto Yoshida</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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