Ancestral amino acid substitution improves the thermal stability of recombinant lignin-peroxidase from white-rot fungi, Phanerochaete chrysosporium strain UAMH 3641.
Identifieur interne : 000281 ( Main/Exploration ); précédent : 000280; suivant : 000282Ancestral amino acid substitution improves the thermal stability of recombinant lignin-peroxidase from white-rot fungi, Phanerochaete chrysosporium strain UAMH 3641.
Auteurs : Yasuyuki Semba [Japon] ; Manabu Ishida [Japon] ; Shin-Ichi Yokobori [Japon] ; Akihiko Yamagishi [Japon]Source :
- Protein engineering, design & selection : PEDS [ 1741-0134 ] ; 2015.
Descripteurs français
- KwdFr :
- Clonage moléculaire (MeSH), Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Modèles moléculaires (MeSH), Mutation (MeSH), Peroxidases (composition chimique), Peroxidases (génétique), Peroxidases (métabolisme), Phanerochaete (enzymologie), Phylogenèse (MeSH), Protéines recombinantes (composition chimique), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Stabilité enzymatique (génétique), Substitution d'acide aminé (MeSH), Séquence d'acides aminés (MeSH), Température (MeSH), Température de transition (MeSH).
- MESH :
- composition chimique : Peroxidases, Protéines recombinantes.
- enzymologie : Phanerochaete.
- génétique : Peroxidases, Protéines recombinantes, Stabilité enzymatique.
- métabolisme : Peroxidases, Protéines recombinantes.
- Clonage moléculaire, Conformation des protéines, Données de séquences moléculaires, Modèles moléculaires, Mutation, Phylogenèse, Substitution d'acide aminé, Séquence d'acides aminés, Température, Température de transition.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amino Acid Substitution (MeSH), Cloning, Molecular (MeSH), Enzyme Stability (genetics), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Mutation (MeSH), Peroxidases (chemistry), Peroxidases (genetics), Peroxidases (metabolism), Phanerochaete (enzymology), Phylogeny (MeSH), Protein Conformation (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Temperature (MeSH), Transition Temperature (MeSH).
- MESH :
- chemical , chemistry : Peroxidases, Recombinant Proteins.
- enzymology : Phanerochaete.
- genetics : Enzyme Stability, Peroxidases, Recombinant Proteins.
- chemical , metabolism : Peroxidases, Recombinant Proteins.
- Amino Acid Sequence, Amino Acid Substitution, Cloning, Molecular, Models, Molecular, Molecular Sequence Data, Mutation, Phylogeny, Protein Conformation, Temperature, Transition Temperature.
Abstract
Stabilizing enzymes from mesophiles of industrial interest is one of the greatest challenges of protein engineering. The ancestral mutation method, which introduces inferred ancestral residues into a target enzyme, has previously been developed and used to improve the thermostability of thermophilic enzymes. In this report, we studied the ancestral mutation method to improve the chemical and thermal stabilities of Phanerochaete chrysosporium lignin peroxidase (LiP), a mesophilic fungal enzyme. A fungal ancestral LiP sequence was inferred using a phylogenetic tree comprising Basidiomycota and Ascomycota fungal peroxidase sequences. Eleven mutant enzymes containing ancestral residues were designed, heterologously expressed in Escherichia coli and purified. Several of these ancestral mutants showed higher thermal stabilities and increased specific activities and/or kcat/KM than those of wild-type LiP.
DOI: 10.1093/protein/gzv023
PubMed: 25858964
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Ishida, Manabu" sort="Ishida, Manabu" uniqKey="Ishida M" first="Manabu" last="Ishida">Manabu Ishida</name><affiliation wicri:level="1"><nlm:affiliation>Department of Applied Biology, Faculty of Life Science, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo 192-0392, Japan Top Runner Incubation Center for Academia-Industry Fusion, Department of Bioengineering, Faculty of Engineering, Nagaoka University of Technology, 1603-1, Kamitomiokamachi, Nagaoka, Niigata 940-2188, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Applied Biology, Faculty of Life Science, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo 192-0392, Japan Top Runner Incubation Center for Academia-Industry Fusion, Department of Bioengineering, Faculty of Engineering, Nagaoka University of Technology, 1603-1, Kamitomiokamachi, Nagaoka, Niigata 940-2188</wicri:regionArea><wicri:noRegion>Niigata 940-2188</wicri:noRegion></affiliation></author><author><name sortKey="Yokobori, Shin Ichi" sort="Yokobori, Shin Ichi" uniqKey="Yokobori S" first="Shin-Ichi" last="Yokobori">Shin-Ichi Yokobori</name><affiliation wicri:level="1"><nlm:affiliation>Department of Applied Biology, Faculty of Life Science, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo 192-0392, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Applied Biology, Faculty of Life Science, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo 192-0392</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author><author><name sortKey="Yamagishi, Akihiko" sort="Yamagishi, Akihiko" uniqKey="Yamagishi A" first="Akihiko" last="Yamagishi">Akihiko Yamagishi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Applied Biology, Faculty of Life Science, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo 192-0392, Japan yamagish@toyaku.ac.jp yamagish@ls.toyaku.ac.jp.</nlm:affiliation><country wicri:rule="url">Japon</country><wicri:regionArea>Department of Applied Biology, Faculty of Life Science, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo 192-0392</wicri:regionArea><placeName><settlement type="city">Tokyo</settlement><region type="région">Région de Kantō</region></placeName></affiliation></author></analytic><series><title level="j">Protein engineering, design & selection : PEDS</title><idno type="eISSN">1741-0134</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Amino Acid Substitution (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Enzyme Stability (genetics)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutation (MeSH)</term><term>Peroxidases (chemistry)</term><term>Peroxidases (genetics)</term><term>Peroxidases (metabolism)</term><term>Phanerochaete (enzymology)</term><term>Phylogeny (MeSH)</term><term>Protein Conformation (MeSH)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Temperature (MeSH)</term><term>Transition Temperature (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Clonage moléculaire (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Mutation (MeSH)</term><term>Peroxidases (composition chimique)</term><term>Peroxidases (génétique)</term><term>Peroxidases (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Phylogenèse (MeSH)</term><term>Protéines recombinantes (composition chimique)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Stabilité enzymatique (génétique)</term><term>Substitution d'acide aminé (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Température (MeSH)</term><term>Température de transition (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Peroxidases</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="genetics" xml:lang="en"><term>Enzyme Stability</term><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Peroxidases</term><term>Protéines recombinantes</term><term>Stabilité enzymatique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peroxidases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Peroxidases</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Cloning, Molecular</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Phylogeny</term><term>Protein Conformation</term><term>Temperature</term><term>Transition Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Clonage moléculaire</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Mutation</term><term>Phylogenèse</term><term>Substitution d'acide aminé</term><term>Séquence d'acides aminés</term><term>Température</term><term>Température de transition</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Stabilizing enzymes from mesophiles of industrial interest is one of the greatest challenges of protein engineering. The ancestral mutation method, which introduces inferred ancestral residues into a target enzyme, has previously been developed and used to improve the thermostability of thermophilic enzymes. In this report, we studied the ancestral mutation method to improve the chemical and thermal stabilities of Phanerochaete chrysosporium lignin peroxidase (LiP), a mesophilic fungal enzyme. A fungal ancestral LiP sequence was inferred using a phylogenetic tree comprising Basidiomycota and Ascomycota fungal peroxidase sequences. Eleven mutant enzymes containing ancestral residues were designed, heterologously expressed in Escherichia coli and purified. Several of these ancestral mutants showed higher thermal stabilities and increased specific activities and/or kcat/KM than those of wild-type LiP. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25858964</PMID><DateCompleted><Year>2016</Year><Month>03</Month><Day>11</Day></DateCompleted><DateRevised><Year>2015</Year><Month>06</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1741-0134</ISSN><JournalIssue CitedMedium="Internet"><Volume>28</Volume><Issue>7</Issue><PubDate><Year>2015</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Protein engineering, design & selection : PEDS</Title><ISOAbbreviation>Protein Eng Des Sel</ISOAbbreviation></Journal><ArticleTitle>Ancestral amino acid substitution improves the thermal stability of recombinant lignin-peroxidase from white-rot fungi, Phanerochaete chrysosporium strain UAMH 3641.</ArticleTitle><Pagination><MedlinePgn>221-30</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/protein/gzv023</ELocationID><Abstract><AbstractText>Stabilizing enzymes from mesophiles of industrial interest is one of the greatest challenges of protein engineering. The ancestral mutation method, which introduces inferred ancestral residues into a target enzyme, has previously been developed and used to improve the thermostability of thermophilic enzymes. In this report, we studied the ancestral mutation method to improve the chemical and thermal stabilities of Phanerochaete chrysosporium lignin peroxidase (LiP), a mesophilic fungal enzyme. A fungal ancestral LiP sequence was inferred using a phylogenetic tree comprising Basidiomycota and Ascomycota fungal peroxidase sequences. Eleven mutant enzymes containing ancestral residues were designed, heterologously expressed in Escherichia coli and purified. Several of these ancestral mutants showed higher thermal stabilities and increased specific activities and/or kcat/KM than those of wild-type LiP. </AbstractText><CopyrightInformation>© The Author 2015. Published by Oxford University Press. All rights reserved. For Permissions, please e-mail: journals.permissions@oup.com.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Semba</LastName><ForeName>Yasuyuki</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Applied Biology, Faculty of Life Science, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo 192-0392, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ishida</LastName><ForeName>Manabu</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Applied Biology, Faculty of Life Science, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo 192-0392, Japan Top Runner Incubation Center for Academia-Industry Fusion, Department of Bioengineering, Faculty of Engineering, Nagaoka University of Technology, 1603-1, Kamitomiokamachi, Nagaoka, Niigata 940-2188, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yokobori</LastName><ForeName>Shin-ichi</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Applied Biology, Faculty of Life Science, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo 192-0392, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yamagishi</LastName><ForeName>Akihiko</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Applied Biology, Faculty of Life Science, Tokyo University of Pharmacy and Life Sciences, 1432-1, Horinouchi, Hachioji, Tokyo 192-0392, Japan yamagish@toyaku.ac.jp yamagish@ls.toyaku.ac.jp.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>04</Month><Day>08</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Protein Eng Des Sel</MedlineTA><NlmUniqueID>101186484</NlmUniqueID><ISSNLinking>1741-0126</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="Y">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004795" MajorTopicYN="N">Enzyme Stability</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013696" MajorTopicYN="Y">Temperature</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D044366" MajorTopicYN="N">Transition Temperature</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Phanerochaete chrysosporium</Keyword><Keyword MajorTopicYN="N">ancestral mutation method</Keyword><Keyword MajorTopicYN="N">lignin peroxidase</Keyword><Keyword MajorTopicYN="N">thermostabilization</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>06</Month><Day>17</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>03</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>4</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>4</Month><Day>11</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>3</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25858964</ArticleId><ArticleId IdType="pii">gzv023</ArticleId><ArticleId 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