Ancestral amino acid substitution improves the thermal stability of recombinant lignin-peroxidase from white-rot fungi, Phanerochaete chrysosporium strain UAMH 3641.
Identifieur interne : 000257 ( Main/Corpus ); précédent : 000256; suivant : 000258Ancestral amino acid substitution improves the thermal stability of recombinant lignin-peroxidase from white-rot fungi, Phanerochaete chrysosporium strain UAMH 3641.
Auteurs : Yasuyuki Semba ; Manabu Ishida ; Shin-Ichi Yokobori ; Akihiko YamagishiSource :
- Protein engineering, design & selection : PEDS [ 1741-0134 ] ; 2015.
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
Links to Exploration step
pubmed:25858964Le document en format XML
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Bioengineering, Faculty of Engineering, Nagaoka University of Technology, 1603-1, Kamitomiokamachi, Nagaoka, Niigata 940-2188, Japan.</nlm:affiliation></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><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></affiliation></author><author><name sortKey="Yamagishi, Akihiko" sort="Yamagishi, Akihiko" uniqKey="Yamagishi A" first="Akihiko" last="Yamagishi">Akihiko Yamagishi</name><affiliation><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></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:25858964</idno><idno type="pmid">25858964</idno><idno type="doi">10.1093/protein/gzv023</idno><idno type="wicri:Area/Main/Corpus">000257</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000257</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Ancestral amino acid substitution improves the thermal stability of recombinant lignin-peroxidase from white-rot fungi, Phanerochaete chrysosporium strain UAMH 3641.</title><author><name sortKey="Semba, Yasuyuki" sort="Semba, Yasuyuki" uniqKey="Semba Y" first="Yasuyuki" last="Semba">Yasuyuki Semba</name><affiliation><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></affiliation></author><author><name sortKey="Ishida, Manabu" sort="Ishida, Manabu" uniqKey="Ishida M" first="Manabu" last="Ishida">Manabu Ishida</name><affiliation><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></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><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></affiliation></author><author><name sortKey="Yamagishi, Akihiko" sort="Yamagishi, Akihiko" uniqKey="Yamagishi A" first="Akihiko" last="Yamagishi">Akihiko Yamagishi</name><affiliation><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></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="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Peroxidases</term><term>Recombinant Proteins</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" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peroxidases</term><term>Recombinant Proteins</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></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 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