Substrate specificity of lignin peroxidase and a S168W variant of manganese peroxidase.
Identifieur interne : 000A66 ( Main/Exploration ); précédent : 000A65; suivant : 000A67Substrate specificity of lignin peroxidase and a S168W variant of manganese peroxidase.
Auteurs : S L Timofeevski [États-Unis] ; G. Nie ; N S Reading ; S D AustSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 2000.
Descripteurs français
- KwdFr :
- Amorces ADN (génétique), Cinétique (MeSH), Domaine catalytique (génétique), Données de séquences moléculaires (MeSH), Isoenzymes (génétique), Isoenzymes (métabolisme), Oxydoréduction (MeSH), Peroxidases (génétique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Phanerochaete (génétique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Similitude de séquences d'acides aminés (MeSH), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Tryptophane (composition chimique), Variation génétique (MeSH).
- MESH :
- composition chimique : Tryptophane.
- enzymologie : Phanerochaete.
- génétique : Amorces ADN, Domaine catalytique, Isoenzymes, Peroxidases, Phanerochaete, Protéines recombinantes.
- métabolisme : Isoenzymes, Peroxidases, Protéines recombinantes.
- Cinétique, Données de séquences moléculaires, Oxydoréduction, Similitude de séquences d'acides aminés, Spécificité du substrat, Séquence d'acides aminés, Séquence nucléotidique, Variation génétique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Catalytic Domain (genetics), DNA Primers (genetics), Genetic Variation (MeSH), Isoenzymes (genetics), Isoenzymes (metabolism), Kinetics (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Peroxidases (genetics), Peroxidases (metabolism), Phanerochaete (enzymology), Phanerochaete (genetics), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Homology, Amino Acid (MeSH), Substrate Specificity (MeSH), Tryptophan (chemistry).
- MESH :
- chemical , chemistry : Tryptophan.
- chemical , genetics : DNA Primers, Isoenzymes, Peroxidases, Recombinant Proteins.
- enzymology : Phanerochaete.
- genetics : Catalytic Domain, Phanerochaete.
- chemical , metabolism : Isoenzymes, Peroxidases, Recombinant Proteins.
- Amino Acid Sequence, Base Sequence, Genetic Variation, Kinetics, Molecular Sequence Data, Oxidation-Reduction, Sequence Homology, Amino Acid, Substrate Specificity.
Abstract
Lignin peroxidase (LiP) and manganese peroxidase (MnP) are structurally similar heme-containing enzymes secreted by white-rot fungi. Unlike MnP, which is only specific for Mn(2+), LiP has broad substrate specificity, but it is not known if this versatility is due to multiple substrate-binding sites. We report here that a S168W variant of MnP from Phanerochaete chrysosporium not only retained full Mn(2+) oxidase activity, but also, unlike native or recombinant MnP, oxidized a multitude of LiP substrates, including small molecule and polymeric substrates. The kinetics of oxidation of most nonpolymeric substrates by the MnP variant and LiP were similar. The stoichiometries for veratryl alcohol oxidation by these two enzymes were identical. Some readily oxidizable substrates, such as guaiacol and ferrocyanide, were oxidized by MnP S168W and LiP both specifically and nonspecifically while recombinant MnP oxidized these substrates only nonspecifically. The functional similarities between this MnP variant and LiP provide evidence for the broad substrate specificity of a single oxidation site near the surface tryptophan.
DOI: 10.1006/abbi.1999.1562
PubMed: 10620333
Affiliations:
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Nie</name></author><author><name sortKey="Reading, N S" sort="Reading, N S" uniqKey="Reading N" first="N S" last="Reading">N S Reading</name></author><author><name sortKey="Aust, S D" sort="Aust, S D" uniqKey="Aust S" first="S D" last="Aust">S D Aust</name></author></analytic><series><title level="j">Archives of biochemistry and biophysics</title><idno type="ISSN">0003-9861</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>Catalytic Domain (genetics)</term><term>DNA Primers (genetics)</term><term>Genetic Variation (MeSH)</term><term>Isoenzymes (genetics)</term><term>Isoenzymes (metabolism)</term><term>Kinetics (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Phanerochaete (genetics)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Substrate Specificity (MeSH)</term><term>Tryptophan (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN (génétique)</term><term>Cinétique (MeSH)</term><term>Domaine catalytique (génétique)</term><term>Données de séquences moléculaires (MeSH)</term><term>Isoenzymes (génétique)</term><term>Isoenzymes (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Phanerochaete (génétique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Spécificité du substrat (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term><term>Tryptophane (composition chimique)</term><term>Variation génétique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Tryptophan</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA Primers</term><term>Isoenzymes</term><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Tryptophane</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="genetics" xml:lang="en"><term>Catalytic Domain</term><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Amorces ADN</term><term>Domaine catalytique</term><term>Isoenzymes</term><term>Peroxidases</term><term>Phanerochaete</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Isoenzymes</term><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Isoenzymes</term><term>Peroxidases</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Genetic Variation</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Sequence Homology, Amino Acid</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Données de séquences moléculaires</term><term>Oxydoréduction</term><term>Similitude de séquences d'acides aminés</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Variation génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lignin peroxidase (LiP) and manganese peroxidase (MnP) are structurally similar heme-containing enzymes secreted by white-rot fungi. Unlike MnP, which is only specific for Mn(2+), LiP has broad substrate specificity, but it is not known if this versatility is due to multiple substrate-binding sites. We report here that a S168W variant of MnP from Phanerochaete chrysosporium not only retained full Mn(2+) oxidase activity, but also, unlike native or recombinant MnP, oxidized a multitude of LiP substrates, including small molecule and polymeric substrates. The kinetics of oxidation of most nonpolymeric substrates by the MnP variant and LiP were similar. The stoichiometries for veratryl alcohol oxidation by these two enzymes were identical. Some readily oxidizable substrates, such as guaiacol and ferrocyanide, were oxidized by MnP S168W and LiP both specifically and nonspecifically while recombinant MnP oxidized these substrates only nonspecifically. The functional similarities between this MnP variant and LiP provide evidence for the broad substrate specificity of a single oxidation site near the surface tryptophan.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10620333</PMID><DateCompleted><Year>2000</Year><Month>02</Month><Day>09</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>373</Volume><Issue>1</Issue><PubDate><Year>2000</Year><Month>Jan</Month><Day>01</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Substrate specificity of lignin peroxidase and a S168W variant of manganese peroxidase.</ArticleTitle><Pagination><MedlinePgn>147-53</MedlinePgn></Pagination><Abstract><AbstractText>Lignin peroxidase (LiP) and manganese peroxidase (MnP) are structurally similar heme-containing enzymes secreted by white-rot fungi. Unlike MnP, which is only specific for Mn(2+), LiP has broad substrate specificity, but it is not known if this versatility is due to multiple substrate-binding sites. We report here that a S168W variant of MnP from Phanerochaete chrysosporium not only retained full Mn(2+) oxidase activity, but also, unlike native or recombinant MnP, oxidized a multitude of LiP substrates, including small molecule and polymeric substrates. The kinetics of oxidation of most nonpolymeric substrates by the MnP variant and LiP were similar. The stoichiometries for veratryl alcohol oxidation by these two enzymes were identical. Some readily oxidizable substrates, such as guaiacol and ferrocyanide, were oxidized by MnP S168W and LiP both specifically and nonspecifically while recombinant MnP oxidized these substrates only nonspecifically. The functional similarities between this MnP variant and LiP provide evidence for the broad substrate specificity of a single oxidation site near the surface tryptophan.</AbstractText><CopyrightInformation>Copyright 2000 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="D003160">Comparative Study</PublicationType><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>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007527">Isoenzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014644" MajorTopicYN="N">Genetic Variation</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>1</Month><Day>6</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2000</Year><Month>1</Month><Day>6</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>1</Month><Day>6</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10620333</ArticleId><ArticleId IdType="doi">10.1006/abbi.1999.1562</ArticleId><ArticleId IdType="pii">S0003-9861(99)91562-X</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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