Purification and properties of an aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium.
Identifieur interne : 000F03 ( Main/Exploration ); précédent : 000F02; suivant : 000F04Purification and properties of an aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium.
Auteurs : A. Muheim [Suisse] ; R. Waldner ; D. Sanglard ; J. Reiser ; H E Schoemaker ; M S LeisolaSource :
- European journal of biochemistry [ 0014-2956 ] ; 1991.
Descripteurs français
- KwdFr :
- Alcohol oxidoreductases (composition chimique), Alcohol oxidoreductases (isolement et purification), Alcools benzyliques (métabolisme), Aldéhydes (métabolisme), Champignons (effets des médicaments et des substances chimiques), Champignons (enzymologie), Concentration en ions d'hydrogène (MeSH), Inhibiteurs de la synthèse protéique (pharmacologie), Lignine (métabolisme), Masse moléculaire (MeSH), NADP (métabolisme), Spécificité du substrat (MeSH), Stabilité enzymatique (MeSH), Électrophorèse sur gel de polyacrylamide (MeSH).
- MESH :
- composition chimique : Alcohol oxidoreductases.
- effets des médicaments et des substances chimiques : Champignons.
- enzymologie : Champignons.
- isolement et purification : Alcohol oxidoreductases.
- métabolisme : Alcools benzyliques, Aldéhydes, Lignine, NADP.
- pharmacologie : Inhibiteurs de la synthèse protéique.
- Concentration en ions d'hydrogène, Masse moléculaire, Spécificité du substrat, Stabilité enzymatique, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (chemistry), Alcohol Oxidoreductases (isolation & purification), Aldehydes (metabolism), Benzyl Alcohols (metabolism), Electrophoresis, Polyacrylamide Gel (MeSH), Enzyme Stability (MeSH), Fungi (drug effects), Fungi (enzymology), Hydrogen-Ion Concentration (MeSH), Lignin (metabolism), Molecular Weight (MeSH), NADP (metabolism), Protein Synthesis Inhibitors (pharmacology), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Alcohol Oxidoreductases.
- chemical , isolation & purification : Alcohol Oxidoreductases.
- chemical , metabolism : Aldehydes, Benzyl Alcohols, Lignin, NADP.
- drug effects : Fungi.
- enzymology : Fungi.
- chemical , pharmacology : Protein Synthesis Inhibitors.
- Electrophoresis, Polyacrylamide Gel, Enzyme Stability, Hydrogen-Ion Concentration, Molecular Weight, Substrate Specificity.
Abstract
An intracellular aryl-alcohol dehydrogenase (previously referred to as aryl-aldehyde reductase) was purified from the white-rot fungus Phanerochaete chrysosporium. The enzyme reduced veratraldehyde to veratryl alcohol using NADPH as a cofactor. Other aromatic benzaldehydes were also reduced, but not aromatic ketones. Methoxy-substituted rings were better substrates than hydroxylated ones. The enzyme was also able to reduce a dimeric aldehyde (4-benzyloxy-3-methoxybenzaldehyde). The highest reduction rate was measured when 3,5-dimethoxybenzaldehyde was used as a substrate. On SDS/PAGE the purified enzyme showed one major band with a molecular mass of 47 kDa, whereas gel filtration suggested a molecular mass of 280 kDa. Polyclonal antibodies raised against the gel purified 47-kDa protein were able to immunoprecipitate the aryl-alcohol dehydrogenase indicating that its activity possibly resides entirely in this protein fragment. The pI of the enzyme was 5.2 and it was most active at pH 6.1. The aryl-alcohol dehydrogenase was partially inhibited by typical oxidoreductase inhibitors.
DOI: 10.1111/j.1432-1033.1991.tb15715.x
PubMed: 1997322
Affiliations:
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Le document en format XML
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Reiser</name></author><author><name sortKey="Schoemaker, H E" sort="Schoemaker, H E" uniqKey="Schoemaker H" first="H E" last="Schoemaker">H E Schoemaker</name></author><author><name sortKey="Leisola, M S" sort="Leisola, M S" uniqKey="Leisola M" first="M S" last="Leisola">M S Leisola</name></author></analytic><series><title level="j">European journal of biochemistry</title><idno type="ISSN">0014-2956</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (chemistry)</term><term>Alcohol Oxidoreductases (isolation & purification)</term><term>Aldehydes (metabolism)</term><term>Benzyl Alcohols (metabolism)</term><term>Electrophoresis, Polyacrylamide Gel (MeSH)</term><term>Enzyme Stability (MeSH)</term><term>Fungi (drug effects)</term><term>Fungi (enzymology)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Lignin (metabolism)</term><term>Molecular Weight (MeSH)</term><term>NADP (metabolism)</term><term>Protein Synthesis Inhibitors (pharmacology)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alcohol oxidoreductases (composition chimique)</term><term>Alcohol oxidoreductases (isolement et purification)</term><term>Alcools benzyliques (métabolisme)</term><term>Aldéhydes (métabolisme)</term><term>Champignons (effets des médicaments et des substances chimiques)</term><term>Champignons (enzymologie)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Inhibiteurs de la synthèse protéique (pharmacologie)</term><term>Lignine (métabolisme)</term><term>Masse moléculaire (MeSH)</term><term>NADP (métabolisme)</term><term>Spécificité du substrat (MeSH)</term><term>Stabilité enzymatique (MeSH)</term><term>Électrophorèse sur gel de polyacrylamide (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Alcohol Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Alcohol Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aldehydes</term><term>Benzyl Alcohols</term><term>Lignin</term><term>NADP</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Alcohol oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Champignons</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Champignons</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Alcohol oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcools benzyliques</term><term>Aldéhydes</term><term>Lignine</term><term>NADP</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Inhibiteurs de la synthèse protéique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Protein Synthesis Inhibitors</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electrophoresis, Polyacrylamide Gel</term><term>Enzyme Stability</term><term>Hydrogen-Ion Concentration</term><term>Molecular Weight</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Concentration en ions d'hydrogène</term><term>Masse moléculaire</term><term>Spécificité du substrat</term><term>Stabilité enzymatique</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">An intracellular aryl-alcohol dehydrogenase (previously referred to as aryl-aldehyde reductase) was purified from the white-rot fungus Phanerochaete chrysosporium. The enzyme reduced veratraldehyde to veratryl alcohol using NADPH as a cofactor. Other aromatic benzaldehydes were also reduced, but not aromatic ketones. Methoxy-substituted rings were better substrates than hydroxylated ones. The enzyme was also able to reduce a dimeric aldehyde (4-benzyloxy-3-methoxybenzaldehyde). The highest reduction rate was measured when 3,5-dimethoxybenzaldehyde was used as a substrate. On SDS/PAGE the purified enzyme showed one major band with a molecular mass of 47 kDa, whereas gel filtration suggested a molecular mass of 280 kDa. Polyclonal antibodies raised against the gel purified 47-kDa protein were able to immunoprecipitate the aryl-alcohol dehydrogenase indicating that its activity possibly resides entirely in this protein fragment. The pI of the enzyme was 5.2 and it was most active at pH 6.1. The aryl-alcohol dehydrogenase was partially inhibited by typical oxidoreductase inhibitors.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1997322</PMID><DateCompleted><Year>1991</Year><Month>04</Month><Day>02</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-2956</ISSN><JournalIssue CitedMedium="Print"><Volume>195</Volume><Issue>2</Issue><PubDate><Year>1991</Year><Month>Jan</Month><Day>30</Day></PubDate></JournalIssue><Title>European journal of biochemistry</Title><ISOAbbreviation>Eur J Biochem</ISOAbbreviation></Journal><ArticleTitle>Purification and properties of an aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>369-75</MedlinePgn></Pagination><Abstract><AbstractText>An intracellular aryl-alcohol dehydrogenase (previously referred to as aryl-aldehyde reductase) was purified from the white-rot fungus Phanerochaete chrysosporium. The enzyme reduced veratraldehyde to veratryl alcohol using NADPH as a cofactor. Other aromatic benzaldehydes were also reduced, but not aromatic ketones. Methoxy-substituted rings were better substrates than hydroxylated ones. The enzyme was also able to reduce a dimeric aldehyde (4-benzyloxy-3-methoxybenzaldehyde). The highest reduction rate was measured when 3,5-dimethoxybenzaldehyde was used as a substrate. On SDS/PAGE the purified enzyme showed one major band with a molecular mass of 47 kDa, whereas gel filtration suggested a molecular mass of 280 kDa. Polyclonal antibodies raised against the gel purified 47-kDa protein were able to immunoprecipitate the aryl-alcohol dehydrogenase indicating that its activity possibly resides entirely in this protein fragment. The pI of the enzyme was 5.2 and it was most active at pH 6.1. The aryl-alcohol dehydrogenase was partially inhibited by typical oxidoreductase inhibitors.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Muheim</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Eidgenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Waldner</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Sanglard</LastName><ForeName>D</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Reiser</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Schoemaker</LastName><ForeName>H E</ForeName><Initials>HE</Initials></Author><Author ValidYN="Y"><LastName>Leisola</LastName><ForeName>M S</ForeName><Initials>MS</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Eur J Biochem</MedlineTA><NlmUniqueID>0107600</NlmUniqueID><ISSNLinking>0014-2956</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000447">Aldehydes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011500">Protein Synthesis Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.90</RegistryNumber><NameOfSubstance UI="C055882">aryl-alcohol dehydrogenase</NameOfSubstance></Chemical><Chemical><RegistryNumber>MB4T4A711H</RegistryNumber><NameOfSubstance UI="C042197">veratryl alcohol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000429" MajorTopicYN="N">Alcohol Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000447" MajorTopicYN="N">Aldehydes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011500" MajorTopicYN="N">Protein Synthesis Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>1</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>1</Month><Day>30</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>1</Month><Day>30</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1997322</ArticleId><ArticleId IdType="doi">10.1111/j.1432-1033.1991.tb15715.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suisse</li></country><region><li>Canton de Zurich</li></region><settlement><li>Zurich</li></settlement></list><tree><noCountry><name sortKey="Leisola, M S" sort="Leisola, M S" uniqKey="Leisola M" first="M S" last="Leisola">M S Leisola</name><name sortKey="Reiser, J" sort="Reiser, J" uniqKey="Reiser J" first="J" last="Reiser">J. Reiser</name><name sortKey="Sanglard, D" sort="Sanglard, D" uniqKey="Sanglard D" first="D" last="Sanglard">D. Sanglard</name><name sortKey="Schoemaker, H E" sort="Schoemaker, H E" uniqKey="Schoemaker H" first="H E" last="Schoemaker">H E Schoemaker</name><name sortKey="Waldner, R" sort="Waldner, R" uniqKey="Waldner R" first="R" last="Waldner">R. Waldner</name></noCountry><country name="Suisse"><region name="Canton de Zurich"><name sortKey="Muheim, A" sort="Muheim, A" uniqKey="Muheim A" first="A" last="Muheim">A. Muheim</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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