An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity.
Identifieur interne : 000289 ( Main/Exploration ); précédent : 000288; suivant : 000290An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity.
Auteurs : Diana Linke [Allemagne] ; Nicole Lehnert [Allemagne] ; Manfred Nimtz [Allemagne] ; Ralf G. Berger [Allemagne]Source :
- Enzyme and microbial technology [ 1879-0909 ]
Descripteurs français
- KwdFr :
- ADN fongique (génétique), Alcohol oxidoreductases (composition chimique), Alcohol oxidoreductases (génétique), Alcohol oxidoreductases (métabolisme), Concentration en ions d'hydrogène (MeSH), Données de séquences moléculaires (MeSH), Phanerochaete (enzymologie), Phanerochaete (génétique), Protéines fongiques (composition chimique), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Similitude de séquences d'acides aminés (MeSH), Spécificité du substrat (MeSH), Sugar alcohol dehydrogenases (composition chimique), Sugar alcohol dehydrogenases (génétique), Sugar alcohol dehydrogenases (métabolisme), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Alcohol oxidoreductases, Protéines fongiques, Sugar alcohol dehydrogenases.
- enzymologie : Phanerochaete.
- génétique : ADN fongique, Alcohol oxidoreductases, Phanerochaete, Protéines fongiques, Sugar alcohol dehydrogenases.
- métabolisme : Alcohol oxidoreductases, Protéines fongiques, Sugar alcohol dehydrogenases.
- Concentration en ions d'hydrogène, Données de séquences moléculaires, Similitude de séquences d'acides aminés, Spécificité du substrat, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (chemistry), Alcohol Oxidoreductases (genetics), Alcohol Oxidoreductases (metabolism), Amino Acid Sequence (MeSH), Base Sequence (MeSH), DNA, Fungal (genetics), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Hydrogen-Ion Concentration (MeSH), Molecular Sequence Data (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Sequence Homology, Amino Acid (MeSH), Substrate Specificity (MeSH), Sugar Alcohol Dehydrogenases (chemistry), Sugar Alcohol Dehydrogenases (genetics), Sugar Alcohol Dehydrogenases (metabolism).
- MESH :
- chemical , chemistry : Alcohol Oxidoreductases, Fungal Proteins, Sugar Alcohol Dehydrogenases.
- chemical , genetics : Alcohol Oxidoreductases, DNA, Fungal, Fungal Proteins, Sugar Alcohol Dehydrogenases.
- chemical , metabolism : Alcohol Oxidoreductases, Fungal Proteins, Sugar Alcohol Dehydrogenases.
- enzymology : Phanerochaete.
- genetics : Phanerochaete.
- Amino Acid Sequence, Base Sequence, Hydrogen-Ion Concentration, Molecular Sequence Data, Sequence Homology, Amino Acid, Substrate Specificity.
Abstract
An intracellular alcohol oxidase (AOX) was isolated from the white-rot basidiomycete Phanerochaete chrysosporium (Pch), grown on l-lactate induction medium, and purified to electrophoretic homogeneity. The dimeric protein consisted of two identical 75kDa subunits. The open reading frame of 1,956bp resulted in a monomer consisting of 651 amino acids. The enzyme showed a pI at 5.4, a pH optimum of 9, a temperature optimum at 50°C, possessed putative conserved domains of the GMC superfamily, a FAD binding domain, and showed up to 86% homology to alcohol oxidase sequences of Gloeophyllum trabeum and Coprinopsis cinerea. As was shown for the first time for an AOX from a basidiomycete, not only methanol, but also lower primary alcohols and glycerol were accepted as substrates. An assay based on aldehyde dehydrogenase confirmed d-glyceraldehyde as the product of the reaction. A bioprocess based on this enzyme could alleviate the problems associated with the huge side-stream of glycerol occurring during the manufacture of biodiesel, yielding the green oxidant hydrogen peroxide.
DOI: 10.1016/j.enzmictec.2014.04.001
PubMed: 24910330
Affiliations:
Links toward previous steps (curation, corpus...)
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Electronic address: Diana.linke@lci.uni-hannover.de.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Hanovre</settlement></placeName></affiliation></author><author><name sortKey="Lehnert, Nicole" sort="Lehnert, Nicole" uniqKey="Lehnert N" first="Nicole" last="Lehnert">Nicole Lehnert</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Hanovre</settlement></placeName></affiliation></author><author><name sortKey="Nimtz, Manfred" sort="Nimtz, Manfred" uniqKey="Nimtz M" first="Manfred" last="Nimtz">Manfred Nimtz</name><affiliation wicri:level="1"><nlm:affiliation>Helmholtz Zentrum für Infektionsforschung, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Helmholtz Zentrum für Infektionsforschung, Inhoffenstrasse 7, D-38124 Braunschweig</wicri:regionArea><wicri:noRegion>38124 Braunschweig</wicri:noRegion><wicri:noRegion>38124 Braunschweig</wicri:noRegion><wicri:noRegion>D-38124 Braunschweig</wicri:noRegion></affiliation></author><author><name sortKey="Berger, Ralf G" sort="Berger, Ralf G" uniqKey="Berger R" first="Ralf G" last="Berger">Ralf G. Berger</name><affiliation wicri:level="3"><nlm:affiliation>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover</wicri:regionArea><placeName><region type="land" nuts="2">Basse-Saxe</region><settlement type="city">Hanovre</settlement></placeName></affiliation></author></analytic><series><title level="j">Enzyme and microbial technology</title><idno type="eISSN">1879-0909</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (chemistry)</term><term>Alcohol Oxidoreductases (genetics)</term><term>Alcohol Oxidoreductases (metabolism)</term><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>DNA, Fungal (genetics)</term><term>Fungal Proteins (chemistry)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Sugar Alcohol Dehydrogenases (chemistry)</term><term>Sugar Alcohol Dehydrogenases (genetics)</term><term>Sugar Alcohol Dehydrogenases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN fongique (génétique)</term><term>Alcohol oxidoreductases (composition chimique)</term><term>Alcohol oxidoreductases (génétique)</term><term>Alcohol oxidoreductases (métabolisme)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Protéines fongiques (composition chimique)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Sugar alcohol dehydrogenases (composition chimique)</term><term>Sugar alcohol dehydrogenases (génétique)</term><term>Sugar alcohol dehydrogenases (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Fungal Proteins</term><term>Sugar Alcohol Dehydrogenases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>DNA, Fungal</term><term>Fungal Proteins</term><term>Sugar Alcohol Dehydrogenases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term><term>Fungal Proteins</term><term>Sugar Alcohol Dehydrogenases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Protéines fongiques</term><term>Sugar alcohol dehydrogenases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN fongique</term><term>Alcohol oxidoreductases</term><term>Phanerochaete</term><term>Protéines fongiques</term><term>Sugar alcohol dehydrogenases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Protéines fongiques</term><term>Sugar alcohol dehydrogenases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Hydrogen-Ion Concentration</term><term>Molecular Sequence Data</term><term>Sequence Homology, Amino Acid</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Données de séquences moléculaires</term><term>Similitude de séquences d'acides aminés</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">An intracellular alcohol oxidase (AOX) was isolated from the white-rot basidiomycete Phanerochaete chrysosporium (Pch), grown on l-lactate induction medium, and purified to electrophoretic homogeneity. The dimeric protein consisted of two identical 75kDa subunits. The open reading frame of 1,956bp resulted in a monomer consisting of 651 amino acids. The enzyme showed a pI at 5.4, a pH optimum of 9, a temperature optimum at 50°C, possessed putative conserved domains of the GMC superfamily, a FAD binding domain, and showed up to 86% homology to alcohol oxidase sequences of Gloeophyllum trabeum and Coprinopsis cinerea. As was shown for the first time for an AOX from a basidiomycete, not only methanol, but also lower primary alcohols and glycerol were accepted as substrates. An assay based on aldehyde dehydrogenase confirmed d-glyceraldehyde as the product of the reaction. A bioprocess based on this enzyme could alleviate the problems associated with the huge side-stream of glycerol occurring during the manufacture of biodiesel, yielding the green oxidant hydrogen peroxide. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24910330</PMID><DateCompleted><Year>2015</Year><Month>05</Month><Day>11</Day></DateCompleted><DateRevised><Year>2014</Year><Month>06</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-0909</ISSN><JournalIssue CitedMedium="Internet"><Volume>61-62</Volume><PubDate><MedlineDate>2014 Jul-Aug</MedlineDate></PubDate></JournalIssue><Title>Enzyme and microbial technology</Title><ISOAbbreviation>Enzyme Microb Technol</ISOAbbreviation></Journal><ArticleTitle>An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity.</ArticleTitle><Pagination><MedlinePgn>7-12</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.enzmictec.2014.04.001</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0141-0229(14)00074-X</ELocationID><Abstract><AbstractText>An intracellular alcohol oxidase (AOX) was isolated from the white-rot basidiomycete Phanerochaete chrysosporium (Pch), grown on l-lactate induction medium, and purified to electrophoretic homogeneity. The dimeric protein consisted of two identical 75kDa subunits. The open reading frame of 1,956bp resulted in a monomer consisting of 651 amino acids. The enzyme showed a pI at 5.4, a pH optimum of 9, a temperature optimum at 50°C, possessed putative conserved domains of the GMC superfamily, a FAD binding domain, and showed up to 86% homology to alcohol oxidase sequences of Gloeophyllum trabeum and Coprinopsis cinerea. As was shown for the first time for an AOX from a basidiomycete, not only methanol, but also lower primary alcohols and glycerol were accepted as substrates. An assay based on aldehyde dehydrogenase confirmed d-glyceraldehyde as the product of the reaction. A bioprocess based on this enzyme could alleviate the problems associated with the huge side-stream of glycerol occurring during the manufacture of biodiesel, yielding the green oxidant hydrogen peroxide. </AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Linke</LastName><ForeName>Diana</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover, Germany. Electronic address: Diana.linke@lci.uni-hannover.de.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lehnert</LastName><ForeName>Nicole</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nimtz</LastName><ForeName>Manfred</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Helmholtz Zentrum für Infektionsforschung, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Berger</LastName><ForeName>Ralf G</ForeName><Initials>RG</Initials><AffiliationInfo><Affiliation>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover, Germany.</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>2014</Year><Month>04</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Enzyme Microb Technol</MedlineTA><NlmUniqueID>8003761</NlmUniqueID><ISSNLinking>0141-0229</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004271">DNA, Fungal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D013401">Sugar Alcohol Dehydrogenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.-</RegistryNumber><NameOfSubstance UI="C036131">glycerol oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.13</RegistryNumber><NameOfSubstance UI="C019643">alcohol oxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004271" MajorTopicYN="N">DNA, Fungal</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013401" MajorTopicYN="N">Sugar Alcohol Dehydrogenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Alcohol oxidase</Keyword><Keyword MajorTopicYN="N">Glycerol</Keyword><Keyword MajorTopicYN="N">Phanerochaete chrysosporium</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>10</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>02</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>04</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>6</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>6</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>5</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24910330</ArticleId><ArticleId IdType="pii">S0141-0229(14)00074-X</ArticleId><ArticleId IdType="doi">10.1016/j.enzmictec.2014.04.001</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Basse-Saxe</li></region><settlement><li>Hanovre</li></settlement></list><tree><country name="Allemagne"><region name="Basse-Saxe"><name sortKey="Linke, Diana" sort="Linke, Diana" uniqKey="Linke D" first="Diana" last="Linke">Diana Linke</name></region><name sortKey="Berger, Ralf G" sort="Berger, Ralf G" uniqKey="Berger R" first="Ralf G" last="Berger">Ralf G. Berger</name><name sortKey="Lehnert, Nicole" sort="Lehnert, Nicole" uniqKey="Lehnert N" first="Nicole" last="Lehnert">Nicole Lehnert</name><name sortKey="Nimtz, Manfred" sort="Nimtz, Manfred" uniqKey="Nimtz M" first="Manfred" last="Nimtz">Manfred Nimtz</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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