Cloning and heterologous expression of two aryl-aldehyde dehydrogenases from the white-rot basidiomycete Phanerochaete chrysosporium.
Identifieur interne : 000578 ( Main/Exploration ); précédent : 000577; suivant : 000579Cloning and heterologous expression of two aryl-aldehyde dehydrogenases from the white-rot basidiomycete Phanerochaete chrysosporium.
Auteurs : Tomofumi Nakamura [Japon] ; Hirofumi Ichinose ; Hiroyuki WariishiSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2010.
Descripteurs français
- KwdFr :
- ADN complémentaire (génétique), Aldehyde dehydrogenase (composition chimique), Aldehyde dehydrogenase (génétique), Aldehyde dehydrogenase (métabolisme), Catalyse (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Lignine (métabolisme), Phanerochaete (enzymologie), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéomique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Aldehyde dehydrogenase, Protéines recombinantes.
- enzymologie : Phanerochaete.
- génétique : ADN complémentaire, Aldehyde dehydrogenase, Protéines recombinantes.
- métabolisme : Aldehyde dehydrogenase, Lignine, Protéines recombinantes.
- Catalyse, Clonage moléculaire, Données de séquences moléculaires, Protéomique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Aldehyde Dehydrogenase (chemistry), Aldehyde Dehydrogenase (genetics), Aldehyde Dehydrogenase (metabolism), Amino Acid Sequence (MeSH), Catalysis (MeSH), Cloning, Molecular (MeSH), DNA, Complementary (genetics), Lignin (metabolism), Molecular Sequence Data (MeSH), Phanerochaete (enzymology), Proteomics (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism).
- MESH :
- chemical , chemistry : Aldehyde Dehydrogenase, Recombinant Proteins.
- chemical , genetics : Aldehyde Dehydrogenase, DNA, Complementary, Recombinant Proteins.
- chemical , metabolism : Aldehyde Dehydrogenase, Lignin, Recombinant Proteins.
- enzymology : Phanerochaete.
- Amino Acid Sequence, Catalysis, Cloning, Molecular, Molecular Sequence Data, Proteomics.
Abstract
We identified two aryl-aldehyde dehydrogenase proteins (PcALDH1 and PcALDH2) from the white-rot basidiomycete Phanerochaete chrysosporium. Both PcALDHs were translationally up-regulated in response to exogenous addition of vanillin, one of the key aromatic compounds in the pathway of lignin degradation by basidiomycetes. To clarify the catalytic functions of PcALDHs, we isolated full-length cDNAs encoding these proteins and heterologously expressed the recombinant enzymes using a pET/Escherichia coli system. The open reading frames of both PcALDH1 and PcALDH2 consisted of 1503 nucleotides. The deduced amino acid sequences of both proteins showed high homologies with aryl-aldehyde dehydrogenases from other organisms and contained ten conserved domains of ALDHs. Moreover, a novel glycine-rich motif "GxGxxxG" was located at the NAD(+)-binding site. The recombinant PcALDHs catalyzed dehydrogenation reactions of several aryl-aldehyde compounds, including vanillin, to their corresponding aromatic acids. These results strongly suggested that PcALDHs metabolize aryl-aldehyde compounds generated during fungal degradation of lignin and various aromatic xenobiotics.
DOI: 10.1016/j.bbrc.2010.01.131
PubMed: 20175998
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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uniqKey="Ichinose H" first="Hirofumi" last="Ichinose">Hirofumi Ichinose</name></author><author><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20175998</idno><idno type="pmid">20175998</idno><idno type="doi">10.1016/j.bbrc.2010.01.131</idno><idno type="wicri:Area/Main/Corpus">000571</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000571</idno><idno type="wicri:Area/Main/Curation">000571</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000571</idno><idno type="wicri:Area/Main/Exploration">000571</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Cloning and heterologous expression of two aryl-aldehyde dehydrogenases from the white-rot basidiomycete Phanerochaete 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qualifier="metabolism" xml:lang="en"><term>Aldehyde Dehydrogenase</term><term>Lignin</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Aldehyde dehydrogenase</term><term>Protéines recombinantes</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="génétique" xml:lang="fr"><term>ADN complémentaire</term><term>Aldehyde dehydrogenase</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aldehyde dehydrogenase</term><term>Lignine</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Catalysis</term><term>Cloning, Molecular</term><term>Molecular Sequence 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Both PcALDHs were translationally up-regulated in response to exogenous addition of vanillin, one of the key aromatic compounds in the pathway of lignin degradation by basidiomycetes. To clarify the catalytic functions of PcALDHs, we isolated full-length cDNAs encoding these proteins and heterologously expressed the recombinant enzymes using a pET/Escherichia coli system. The open reading frames of both PcALDH1 and PcALDH2 consisted of 1503 nucleotides. The deduced amino acid sequences of both proteins showed high homologies with aryl-aldehyde dehydrogenases from other organisms and contained ten conserved domains of ALDHs. Moreover, a novel glycine-rich motif "GxGxxxG" was located at the NAD(+)-binding site. The recombinant PcALDHs catalyzed dehydrogenation reactions of several aryl-aldehyde compounds, including vanillin, to their corresponding aromatic acids. These results strongly suggested that PcALDHs metabolize aryl-aldehyde compounds generated during fungal degradation of lignin and various aromatic xenobiotics.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20175998</PMID><DateCompleted><Year>2010</Year><Month>05</Month><Day>04</Day></DateCompleted><DateRevised><Year>2010</Year><Month>04</Month><Day>12</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1090-2104</ISSN><JournalIssue CitedMedium="Internet"><Volume>394</Volume><Issue>3</Issue><PubDate><Year>2010</Year><Month>Apr</Month><Day>09</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Cloning and heterologous expression of two aryl-aldehyde dehydrogenases from the white-rot basidiomycete Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>470-5</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbrc.2010.01.131</ELocationID><Abstract><AbstractText>We identified two aryl-aldehyde dehydrogenase proteins (PcALDH1 and PcALDH2) from the white-rot basidiomycete Phanerochaete chrysosporium. Both PcALDHs were translationally up-regulated in response to exogenous addition of vanillin, one of the key aromatic compounds in the pathway of lignin degradation by basidiomycetes. To clarify the catalytic functions of PcALDHs, we isolated full-length cDNAs encoding these proteins and heterologously expressed the recombinant enzymes using a pET/Escherichia coli system. The open reading frames of both PcALDH1 and PcALDH2 consisted of 1503 nucleotides. The deduced amino acid sequences of both proteins showed high homologies with aryl-aldehyde dehydrogenases from other organisms and contained ten conserved domains of ALDHs. Moreover, a novel glycine-rich motif "GxGxxxG" was located at the NAD(+)-binding site. The recombinant PcALDHs catalyzed dehydrogenation reactions of several aryl-aldehyde compounds, including vanillin, to their corresponding aromatic acids. These results strongly suggested that PcALDHs metabolize aryl-aldehyde compounds generated during fungal degradation of lignin and various aromatic xenobiotics.</AbstractText><CopyrightInformation>Copyright 2010. Published by Elsevier Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>Tomofumi</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka 812-8581, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ichinose</LastName><ForeName>Hirofumi</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Wariishi</LastName><ForeName>Hiroyuki</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>02</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>9005-53-2</RegistryNumber><NameOfSubstance UI="D008031">Lignin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.2.1.3</RegistryNumber><NameOfSubstance UI="D000444">Aldehyde Dehydrogenase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000444" MajorTopicYN="N">Aldehyde Dehydrogenase</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="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008031" MajorTopicYN="N">Lignin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></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></MeshHeading><MeshHeading><DescriptorName UI="D040901" MajorTopicYN="N">Proteomics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year><Month>01</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2010</Year><Month>01</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>2</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>2</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>5</Month><Day>5</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20175998</ArticleId><ArticleId IdType="pii">S0006-291X(10)00202-0</ArticleId><ArticleId IdType="doi">10.1016/j.bbrc.2010.01.131</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Kyūshū</li><li>Préfecture de Fukuoka</li></region><settlement><li>Fukuoka</li></settlement><orgName><li>Université de Kyūshū</li></orgName></list><tree><noCountry><name sortKey="Ichinose, Hirofumi" sort="Ichinose, Hirofumi" uniqKey="Ichinose H" first="Hirofumi" last="Ichinose">Hirofumi Ichinose</name><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name></noCountry><country name="Japon"><region name="Kyūshū"><name sortKey="Nakamura, Tomofumi" sort="Nakamura, Tomofumi" uniqKey="Nakamura T" first="Tomofumi" last="Nakamura">Tomofumi Nakamura</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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