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...)
Le document en format XML
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<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>
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<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>
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<term>Fungal Proteins</term>
<term>Sugar Alcohol Dehydrogenases</term>
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<term>DNA, Fungal</term>
<term>Fungal Proteins</term>
<term>Sugar Alcohol Dehydrogenases</term>
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<term>Fungal Proteins</term>
<term>Sugar Alcohol Dehydrogenases</term>
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<term>Protéines fongiques</term>
<term>Sugar alcohol dehydrogenases</term>
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<term>Phanerochaete</term>
<term>Protéines fongiques</term>
<term>Sugar alcohol dehydrogenases</term>
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<term>Protéines fongiques</term>
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<term>Similitude de séquences d'acides aminés</term>
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<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>
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<DateCompleted><Year>2015</Year>
<Month>05</Month>
<Day>11</Day>
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<Title>Enzyme and microbial technology</Title>
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<ArticleTitle>An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity.</ArticleTitle>
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<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>
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<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>
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<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>
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<Author ValidYN="Y"><LastName>Berger</LastName>
<ForeName>Ralf G</ForeName>
<Initials>RG</Initials>
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</MeshHeading>
<MeshHeading><DescriptorName UI="D013401" MajorTopicYN="N">Sugar Alcohol Dehydrogenases</DescriptorName>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Alcohol oxidase</Keyword>
<Keyword MajorTopicYN="N">Glycerol</Keyword>
<Keyword MajorTopicYN="N">Phanerochaete chrysosporium</Keyword>
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<affiliations><list><country><li>Allemagne</li>
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</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>
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