Identification of catalytic residues in glyoxal oxidase by targeted mutagenesis.
Identifieur interne : 000B26 ( Main/Exploration ); précédent : 000B25; suivant : 000B27Identification of catalytic residues in glyoxal oxidase by targeted mutagenesis.
Auteurs : M M Whittaker [États-Unis] ; P J Kersten ; D. Cullen ; J W WhittakerSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1999.
Descripteurs français
- KwdFr :
- Alcohol oxidoreductases (composition chimique), Alcohol oxidoreductases (génétique), Alcohol oxidoreductases (métabolisme), Alignement de séquences (MeSH), Aspergillus nidulans (MeSH), Catalyse (MeSH), Ciblage de gène (MeSH), Données de séquences moléculaires (MeSH), Mutagenèse dirigée (MeSH), Mutation ponctuelle (MeSH), Phanerochaete (MeSH), Pichia (MeSH), Sites de fixation (génétique), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Alcohol oxidoreductases.
- génétique : Alcohol oxidoreductases, Sites de fixation.
- métabolisme : Alcohol oxidoreductases.
- Alignement de séquences, Aspergillus nidulans, Catalyse, Ciblage de gène, Données de séquences moléculaires, Mutagenèse dirigée, Mutation ponctuelle, Phanerochaete, Pichia, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (chemistry), Alcohol Oxidoreductases (genetics), Alcohol Oxidoreductases (metabolism), Amino Acid Sequence (MeSH), Aspergillus nidulans (MeSH), Binding Sites (genetics), Catalysis (MeSH), Gene Targeting (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Phanerochaete (MeSH), Pichia (MeSH), Point Mutation (MeSH), Sequence Alignment (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Alcohol Oxidoreductases.
- chemical , genetics : Alcohol Oxidoreductases.
- chemical , metabolism : Alcohol Oxidoreductases.
- genetics : Binding Sites.
- Amino Acid Sequence, Aspergillus nidulans, Catalysis, Gene Targeting, Molecular Sequence Data, Mutagenesis, Site-Directed, Phanerochaete, Pichia, Point Mutation, Sequence Alignment, Substrate Specificity.
Abstract
Glyoxal oxidase is a copper metalloenzyme produced by the wood-rot fungus Phanerochaete chrysosporium as an essential component of its extracellular lignin degradation pathways. Previous spectroscopic studies on glyoxal oxidase have demonstrated that it contains a free radical-coupled copper active site remarkably similar to that found in another fungal metalloenzyme, galactose oxidase. Alignment of primary structures has allowed four catalytic residues of glyoxal oxidase to be targeted for site-directed mutagenesis in the recombinant protein. Three glyoxal oxidase mutants have been heterologously expressed in both a filamentous fungus (Aspergillus nidulans) and in a methylotrophic yeast (Pichia pastoris), the latter expression system producing as much as 2 g of protein per liter of culture medium under conditions of high density methanol-induced fermentation. Biochemical and spectroscopic characterization of the mutant enzymes supports structural correlations between galactose oxidase and glyoxal oxidase, clearly identifying the catalytically important residues in glyoxal oxidase and demonstrating the functions of each of these residues.
DOI: 10.1074/jbc.274.51.36226
PubMed: 10593910
Affiliations:
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Le document en format XML
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Previous spectroscopic studies on glyoxal oxidase have demonstrated that it contains a free radical-coupled copper active site remarkably similar to that found in another fungal metalloenzyme, galactose oxidase. Alignment of primary structures has allowed four catalytic residues of glyoxal oxidase to be targeted for site-directed mutagenesis in the recombinant protein. Three glyoxal oxidase mutants have been heterologously expressed in both a filamentous fungus (Aspergillus nidulans) and in a methylotrophic yeast (Pichia pastoris), the latter expression system producing as much as 2 g of protein per liter of culture medium under conditions of high density methanol-induced fermentation. Biochemical and spectroscopic characterization of the mutant enzymes supports structural correlations between galactose oxidase and glyoxal oxidase, clearly identifying the catalytically important residues in glyoxal oxidase and demonstrating the functions of each of these residues.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10593910</PMID><DateCompleted><Year>2000</Year><Month>01</Month><Day>27</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>274</Volume><Issue>51</Issue><PubDate><Year>1999</Year><Month>Dec</Month><Day>17</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Identification of catalytic residues in glyoxal oxidase by targeted mutagenesis.</ArticleTitle><Pagination><MedlinePgn>36226-32</MedlinePgn></Pagination><Abstract><AbstractText>Glyoxal oxidase is a copper metalloenzyme produced by the wood-rot fungus Phanerochaete chrysosporium as an essential component of its extracellular lignin degradation pathways. Previous spectroscopic studies on glyoxal oxidase have demonstrated that it contains a free radical-coupled copper active site remarkably similar to that found in another fungal metalloenzyme, galactose oxidase. Alignment of primary structures has allowed four catalytic residues of glyoxal oxidase to be targeted for site-directed mutagenesis in the recombinant protein. Three glyoxal oxidase mutants have been heterologously expressed in both a filamentous fungus (Aspergillus nidulans) and in a methylotrophic yeast (Pichia pastoris), the latter expression system producing as much as 2 g of protein per liter of culture medium under conditions of high density methanol-induced fermentation. Biochemical and spectroscopic characterization of the mutant enzymes supports structural correlations between galactose oxidase and glyoxal oxidase, clearly identifying the catalytically important residues in glyoxal oxidase and demonstrating the functions of each of these residues.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Whittaker</LastName><ForeName>M M</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland, Oregon 97291-1000, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kersten</LastName><ForeName>P J</ForeName><Initials>PJ</Initials></Author><Author ValidYN="Y"><LastName>Cullen</LastName><ForeName>D</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Whittaker</LastName><ForeName>J W</ForeName><Initials>JW</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>GM 46749</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.-</RegistryNumber><NameOfSubstance UI="C052371">glyoxal 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="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001233" MajorTopicYN="N">Aspergillus nidulans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018390" MajorTopicYN="N">Gene Targeting</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010843" MajorTopicYN="N">Pichia</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017354" MajorTopicYN="N">Point Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>12</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>12</Month><Day>14</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>12</Month><Day>14</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10593910</ArticleId><ArticleId IdType="doi">10.1074/jbc.274.51.36226</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Cullen, D" sort="Cullen, D" uniqKey="Cullen D" first="D" last="Cullen">D. Cullen</name><name sortKey="Kersten, P J" sort="Kersten, P J" uniqKey="Kersten P" first="P J" last="Kersten">P J Kersten</name><name sortKey="Whittaker, J W" sort="Whittaker, J W" uniqKey="Whittaker J" first="J W" last="Whittaker">J W Whittaker</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Whittaker, M M" sort="Whittaker, M M" uniqKey="Whittaker M" first="M M" last="Whittaker">M M Whittaker</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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