Addition of veratryl alcohol oxidase activity to manganese peroxidase by site-directed mutagenesis.
Identifieur interne : 000B52 ( Main/Exploration ); précédent : 000B51; suivant : 000B53Addition of veratryl alcohol oxidase activity to manganese peroxidase by site-directed mutagenesis.
Auteurs : S L Timofeevski [États-Unis] ; G. Nie ; N S Reading ; S D AustSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1999.
Descripteurs français
- KwdFr :
- Alcohol oxidoreductases (antagonistes et inhibiteurs), Alcohol oxidoreductases (composition chimique), Alcohol oxidoreductases (génétique), Alcohol oxidoreductases (métabolisme), Alcools benzyliques (métabolisme), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Escherichia coli (génétique), Hème (métabolisme), Isoenzymes (composition chimique), Isoenzymes (génétique), Isoenzymes (métabolisme), Manganèse (métabolisme), Manganèse (pharmacologie), Mutagenèse dirigée (MeSH), Oxalates (métabolisme), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (isolement et purification), Peroxidases (métabolisme), Peroxyde d'hydrogène (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Protéines recombinantes (antagonistes et inhibiteurs), Protéines recombinantes (composition chimique), Protéines recombinantes (isolement et purification), Protéines recombinantes (métabolisme), Sites de fixation (MeSH), Solubilité (MeSH), Spectrophotométrie (MeSH), Spécificité du substrat (MeSH), Stabilité enzymatique (MeSH), Tryptophane (génétique), Tryptophane (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Alcohol oxidoreductases, Protéines recombinantes.
- composition chimique : Alcohol oxidoreductases, Isoenzymes, Peroxidases, Protéines recombinantes.
- enzymologie : Phanerochaete.
- génétique : Alcohol oxidoreductases, Escherichia coli, Isoenzymes, Peroxidases, Phanerochaete, Tryptophane.
- isolement et purification : Peroxidases, Protéines recombinantes.
- métabolisme : Alcohol oxidoreductases, Alcools benzyliques, Hème, Isoenzymes, Manganèse, Oxalates, Peroxidases, Peroxyde d'hydrogène, Protéines recombinantes, Tryptophane.
- pharmacologie : Manganèse.
- Cinétique, Concentration en ions d'hydrogène, Mutagenèse dirigée, Sites de fixation, Solubilité, Spectrophotométrie, Spécificité du substrat, Stabilité enzymatique.
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (antagonists & inhibitors), Alcohol Oxidoreductases (chemistry), Alcohol Oxidoreductases (genetics), Alcohol Oxidoreductases (metabolism), Benzyl Alcohols (metabolism), Binding Sites (MeSH), Enzyme Stability (MeSH), Escherichia coli (genetics), Heme (metabolism), Hydrogen Peroxide (metabolism), Hydrogen-Ion Concentration (MeSH), Isoenzymes (chemistry), Isoenzymes (genetics), Isoenzymes (metabolism), Kinetics (MeSH), Manganese (metabolism), Manganese (pharmacology), Mutagenesis, Site-Directed (MeSH), Oxalates (metabolism), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (isolation & purification), Peroxidases (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Recombinant Proteins (antagonists & inhibitors), Recombinant Proteins (chemistry), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Solubility (MeSH), Spectrophotometry (MeSH), Substrate Specificity (MeSH), Tryptophan (genetics), Tryptophan (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Alcohol Oxidoreductases, Recombinant Proteins.
- chemical , chemistry : Alcohol Oxidoreductases, Isoenzymes, Peroxidases, Recombinant Proteins.
- chemical , genetics : Alcohol Oxidoreductases, Isoenzymes, Peroxidases, Tryptophan.
- chemical , isolation & purification : Peroxidases, Recombinant Proteins.
- chemical , metabolism : Alcohol Oxidoreductases, Benzyl Alcohols, Heme, Hydrogen Peroxide, Isoenzymes, Manganese, Oxalates, Peroxidases, Recombinant Proteins, Tryptophan.
- enzymology : Phanerochaete.
- genetics : Escherichia coli, Phanerochaete.
- chemical , pharmacology : Manganese.
- Binding Sites, Enzyme Stability, Hydrogen-Ion Concentration, Kinetics, Mutagenesis, Site-Directed, Solubility, Spectrophotometry, Substrate Specificity.
Abstract
Manganese peroxidase and lignin peroxidase are ligninolytic heme-containing enzymes secreted by the white-rot fungus Phanerochaete chrysosporium. Despite structural similarity, these peroxidases oxidize different substrates. Veratryl alcohol is a typical substrate for lignin peroxidase, while manganese peroxidase oxidizes chelated Mn2+. By a single mutation, S168W, we have added veratryl alcohol oxidase activity to recombinant manganese peroxidase expressed in Escherichia coli. The kcat for veratryl alcohol oxidation was 11 s-1, Km for veratryl alcohol approximately 0.49 mM, and Km for hydrogen peroxide approximately 25 microM at pH 2.3. The Km for veratryl alcohol was higher and Km for hydrogen peroxide was lower for this manganese peroxidase mutant compared to two recombinant lignin peroxidase isoenzymes. The mutant retained full manganese peroxidase activity and the kcat was approximately 2.6 x 10(2) s-1 at pH 4.3. Consistent with relative activities with respect to these substrates, Mn2+ strongly inhibited veratryl alcohol oxidation. The single productive mutation in manganese peroxidase suggested that this surface tryptophan residue (W171) in lignin peroxidase is involved in catalysis.
DOI: 10.1006/bbrc.1999.0360
PubMed: 10080927
Affiliations:
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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>Escherichia coli</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Escherichia coli</term><term>Isoenzymes</term><term>Peroxidases</term><term>Phanerochaete</term><term>Tryptophane</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Peroxidases</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Alcohol oxidoreductases</term><term>Alcools benzyliques</term><term>Hème</term><term>Isoenzymes</term><term>Manganèse</term><term>Oxalates</term><term>Peroxidases</term><term>Peroxyde d'hydrogène</term><term>Protéines recombinantes</term><term>Tryptophane</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Manganèse</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Manganese</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Binding Sites</term><term>Enzyme Stability</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Mutagenesis, Site-Directed</term><term>Solubility</term><term>Spectrophotometry</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Mutagenèse dirigée</term><term>Sites de fixation</term><term>Solubilité</term><term>Spectrophotométrie</term><term>Spécificité du substrat</term><term>Stabilité enzymatique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Manganese peroxidase and lignin peroxidase are ligninolytic heme-containing enzymes secreted by the white-rot fungus Phanerochaete chrysosporium. Despite structural similarity, these peroxidases oxidize different substrates. Veratryl alcohol is a typical substrate for lignin peroxidase, while manganese peroxidase oxidizes chelated Mn2+. By a single mutation, S168W, we have added veratryl alcohol oxidase activity to recombinant manganese peroxidase expressed in Escherichia coli. The kcat for veratryl alcohol oxidation was 11 s-1, Km for veratryl alcohol approximately 0.49 mM, and Km for hydrogen peroxide approximately 25 microM at pH 2.3. The Km for veratryl alcohol was higher and Km for hydrogen peroxide was lower for this manganese peroxidase mutant compared to two recombinant lignin peroxidase isoenzymes. The mutant retained full manganese peroxidase activity and the kcat was approximately 2.6 x 10(2) s-1 at pH 4.3. Consistent with relative activities with respect to these substrates, Mn2+ strongly inhibited veratryl alcohol oxidation. The single productive mutation in manganese peroxidase suggested that this surface tryptophan residue (W171) in lignin peroxidase is involved in catalysis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10080927</PMID><DateCompleted><Year>1999</Year><Month>04</Month><Day>19</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>256</Volume><Issue>3</Issue><PubDate><Year>1999</Year><Month>Mar</Month><Day>24</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Addition of veratryl alcohol oxidase activity to manganese peroxidase by site-directed mutagenesis.</ArticleTitle><Pagination><MedlinePgn>500-4</MedlinePgn></Pagination><Abstract><AbstractText>Manganese peroxidase and lignin peroxidase are ligninolytic heme-containing enzymes secreted by the white-rot fungus Phanerochaete chrysosporium. Despite structural similarity, these peroxidases oxidize different substrates. Veratryl alcohol is a typical substrate for lignin peroxidase, while manganese peroxidase oxidizes chelated Mn2+. By a single mutation, S168W, we have added veratryl alcohol oxidase activity to recombinant manganese peroxidase expressed in Escherichia coli. The kcat for veratryl alcohol oxidation was 11 s-1, Km for veratryl alcohol approximately 0.49 mM, and Km for hydrogen peroxide approximately 25 microM at pH 2.3. The Km for veratryl alcohol was higher and Km for hydrogen peroxide was lower for this manganese peroxidase mutant compared to two recombinant lignin peroxidase isoenzymes. The mutant retained full manganese peroxidase activity and the kcat was approximately 2.6 x 10(2) s-1 at pH 4.3. Consistent with relative activities with respect to these substrates, Mn2+ strongly inhibited veratryl alcohol oxidation. The single productive mutation in manganese peroxidase suggested that this surface tryptophan residue (W171) in lignin peroxidase is involved in catalysis.</AbstractText><CopyrightInformation>Copyright 1999 Academic Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Timofeevski</LastName><ForeName>S L</ForeName><Initials>SL</Initials><AffiliationInfo><Affiliation>Biotechnology Center, Utah State University, Logan, Utah, 84322-4705, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nie</LastName><ForeName>G</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Reading</LastName><ForeName>N S</ForeName><Initials>NS</Initials></Author><Author ValidYN="Y"><LastName>Aust</LastName><ForeName>S D</ForeName><Initials>SD</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>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001592">Benzyl Alcohols</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010070">Oxalates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>42VZT0U6YR</RegistryNumber><NameOfSubstance UI="D006418">Heme</NameOfSubstance></Chemical><Chemical><RegistryNumber>42Z2K6ZL8P</RegistryNumber><NameOfSubstance UI="D008345">Manganese</NameOfSubstance></Chemical><Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.-</RegistryNumber><NameOfSubstance UI="D000429">Alcohol Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.3.-</RegistryNumber><NameOfSubstance UI="C057990">veratryl alcohol oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="C042858">lignin peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.13</RegistryNumber><NameOfSubstance UI="C051129">manganese peroxidase</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="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><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="D001592" MajorTopicYN="N">Benzyl Alcohols</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006418" MajorTopicYN="N">Heme</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007527" MajorTopicYN="N">Isoenzymes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008345" MajorTopicYN="N">Manganese</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="Y">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010070" MajorTopicYN="N">Oxalates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></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="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012995" MajorTopicYN="N">Solubility</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013053" MajorTopicYN="N">Spectrophotometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>3</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>3</Month><Day>19</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>3</Month><Day>19</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10080927</ArticleId><ArticleId IdType="pii">S0006-291X(99)90360-1</ArticleId><ArticleId IdType="doi">10.1006/bbrc.1999.0360</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name><name sortKey="Nie, G" sort="Nie, G" uniqKey="Nie G" first="G" last="Nie">G. Nie</name><name sortKey="Reading, N S" sort="Reading, N S" uniqKey="Reading N" first="N S" last="Reading">N S Reading</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Timofeevski, S L" sort="Timofeevski, S L" uniqKey="Timofeevski S" first="S L" last="Timofeevski">S L Timofeevski</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:10080927" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a PhanerochaeteV1
| This area was generated with Dilib version V0.6.37. |  |