Structural Features on the Substrate-Binding Surface of Fungal Lytic Polysaccharide Monooxygenases Determine Their Oxidative Regioselectivity.
Identifieur interne : 000051 ( Main/Exploration ); précédent : 000050; suivant : 000052Structural Features on the Substrate-Binding Surface of Fungal Lytic Polysaccharide Monooxygenases Determine Their Oxidative Regioselectivity.
Auteurs : Barbara Danneels [Belgique] ; Magali Tanghe [Belgique] ; Tom Desmet [Belgique]Source :
- Biotechnology journal [ 1860-7314 ] ; 2019.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Champignons, Cuivre, Mixed function oxygenases, Polyosides, Protéines fongiques.
- Oxydoréduction.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Copper, Fungal Proteins, Mixed Function Oxygenases, Polysaccharides.
- metabolism : Fungi.
- Oxidation-Reduction.
Abstract
Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that oxidatively cleave many of nature's most recalcitrant polysaccharides by acting on the C1- and/or C4-carbon of the glycosidic bond. Here, the results of an extensive mutagenesis study on three LPMO representatives, Phanerochaete chrysosporium LPMO9D (C1-oxidizer), Neurospora crassa LPMO9C (C4), and Hypocrea jecorina LPMO9A (C1/C4), are reported. Using a previously published indicator diagram, the authors demonstrate that several structural determinants of LPMOs play an important role in their oxidative regioselectivity. N-glycan removal and alterations of the aromatic residues on the substrate-binding surface are shown to alter C1/C4-oxidation ratios. Removing the carbohydrate binding module (CBM) is found not to alter the regioselectivity of HjLPMO9A, although the effect of mutational changes is shown to increase in a CBM-free context. The accessibility to the solvent-exposed axial position of the copper-site reveales not to be a major regioselectivity indicator, at least not in PcLPMO9D. Interestingly, a HjLPMO9A variant lacking two surface exposed aromatic residues combines decreased binding capacity with a 22% increase in synergetic efficiency. Similarly to recent LPMO10 findings, our results suggest a complex matrix of surface-interactions that enables LPMO9s not only to bind their substrate, but also to accurately direct their oxidative force.
DOI: 10.1002/biot.201800211
PubMed: 30238672
Affiliations:
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University, Coupure links 653, 9000 Ghent</wicri:regionArea><placeName><region type="province" nuts="2">Province de Flandre-Orientale</region><settlement type="city">Gand</settlement></placeName><orgName type="university">Université de Gand</orgName></affiliation></author><author><name sortKey="Desmet, Tom" sort="Desmet, Tom" uniqKey="Desmet T" first="Tom" last="Desmet">Tom Desmet</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biotechnology, Ghent University, Coupure links 653, 9000 Ghent, Belgium.</nlm:affiliation><country xml:lang="fr">Belgique</country><wicri:regionArea>Department of Biotechnology, Ghent University, Coupure links 653, 9000 Ghent</wicri:regionArea><placeName><region type="province" nuts="2">Province de Flandre-Orientale</region><settlement type="city">Gand</settlement></placeName><orgName type="university">Université de Gand</orgName></affiliation></author></analytic><series><title level="j">Biotechnology journal</title><idno type="eISSN">1860-7314</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Copper (metabolism)</term><term>Fungal Proteins (metabolism)</term><term>Fungi (metabolism)</term><term>Mixed Function Oxygenases (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Polysaccharides (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Champignons (métabolisme)</term><term>Cuivre (métabolisme)</term><term>Mixed function oxygenases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Polyosides (métabolisme)</term><term>Protéines fongiques (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Copper</term><term>Fungal Proteins</term><term>Mixed Function Oxygenases</term><term>Polysaccharides</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Fungi</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Champignons</term><term>Cuivre</term><term>Mixed function oxygenases</term><term>Polyosides</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that oxidatively cleave many of nature's most recalcitrant polysaccharides by acting on the C1- and/or C4-carbon of the glycosidic bond. Here, the results of an extensive mutagenesis study on three LPMO representatives, Phanerochaete chrysosporium LPMO9D (C1-oxidizer), Neurospora crassa LPMO9C (C4), and Hypocrea jecorina LPMO9A (C1/C4), are reported. Using a previously published indicator diagram, the authors demonstrate that several structural determinants of LPMOs play an important role in their oxidative regioselectivity. N-glycan removal and alterations of the aromatic residues on the substrate-binding surface are shown to alter C1/C4-oxidation ratios. Removing the carbohydrate binding module (CBM) is found not to alter the regioselectivity of HjLPMO9A, although the effect of mutational changes is shown to increase in a CBM-free context. The accessibility to the solvent-exposed axial position of the copper-site reveales not to be a major regioselectivity indicator, at least not in PcLPMO9D. Interestingly, a HjLPMO9A variant lacking two surface exposed aromatic residues combines decreased binding capacity with a 22% increase in synergetic efficiency. Similarly to recent LPMO10 findings, our results suggest a complex matrix of surface-interactions that enables LPMO9s not only to bind their substrate, but also to accurately direct their oxidative force.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30238672</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>14</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>14</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1860-7314</ISSN><JournalIssue CitedMedium="Internet"><Volume>14</Volume><Issue>3</Issue><PubDate><Year>2019</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Biotechnology journal</Title><ISOAbbreviation>Biotechnol J</ISOAbbreviation></Journal><ArticleTitle>Structural Features on the Substrate-Binding Surface of Fungal Lytic Polysaccharide Monooxygenases Determine Their Oxidative Regioselectivity.</ArticleTitle><Pagination><MedlinePgn>e1800211</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/biot.201800211</ELocationID><Abstract><AbstractText>Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that oxidatively cleave many of nature's most recalcitrant polysaccharides by acting on the C1- and/or C4-carbon of the glycosidic bond. Here, the results of an extensive mutagenesis study on three LPMO representatives, Phanerochaete chrysosporium LPMO9D (C1-oxidizer), Neurospora crassa LPMO9C (C4), and Hypocrea jecorina LPMO9A (C1/C4), are reported. Using a previously published indicator diagram, the authors demonstrate that several structural determinants of LPMOs play an important role in their oxidative regioselectivity. N-glycan removal and alterations of the aromatic residues on the substrate-binding surface are shown to alter C1/C4-oxidation ratios. Removing the carbohydrate binding module (CBM) is found not to alter the regioselectivity of HjLPMO9A, although the effect of mutational changes is shown to increase in a CBM-free context. The accessibility to the solvent-exposed axial position of the copper-site reveales not to be a major regioselectivity indicator, at least not in PcLPMO9D. Interestingly, a HjLPMO9A variant lacking two surface exposed aromatic residues combines decreased binding capacity with a 22% increase in synergetic efficiency. Similarly to recent LPMO10 findings, our results suggest a complex matrix of surface-interactions that enables LPMO9s not only to bind their substrate, but also to accurately direct their oxidative force.</AbstractText><CopyrightInformation>© 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Danneels</LastName><ForeName>Barbara</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Ghent University, Coupure links 653, 9000 Ghent, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tanghe</LastName><ForeName>Magali</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Ghent University, Coupure links 653, 9000 Ghent, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Desmet</LastName><ForeName>Tom</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Ghent University, Coupure links 653, 9000 Ghent, Belgium.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><Agency>Bijzonder Onderzoeksfonds MRP project "Ghent Bio-Economy"</Agency><Country></Country></Grant><Grant><GrantID>PhD-grant 121629</GrantID><Agency>Agentschap voor Innovatie door Wetenschap en Technologie</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>09</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Biotechnol J</MedlineTA><NlmUniqueID>101265833</NlmUniqueID><ISSNLinking>1860-6768</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011134">Polysaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>789U1901C5</RegistryNumber><NameOfSubstance UI="D003300">Copper</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D006899">Mixed Function Oxygenases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003300" MajorTopicYN="N">Copper</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005658" MajorTopicYN="N">Fungi</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006899" MajorTopicYN="N">Mixed Function Oxygenases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Pichia pastoris</Keyword><Keyword MajorTopicYN="N">enzyme engineering</Keyword><Keyword MajorTopicYN="N">lytic polysaccharide monooxygenase</Keyword><Keyword MajorTopicYN="N">oxidative regioselectivity</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>04</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>08</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>9</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>6</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>9</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30238672</ArticleId><ArticleId IdType="doi">10.1002/biot.201800211</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Belgique</li></country><region><li>Province de Flandre-Orientale</li></region><settlement><li>Gand</li></settlement><orgName><li>Université de Gand</li></orgName></list><tree><country name="Belgique"><region name="Province de Flandre-Orientale"><name sortKey="Danneels, Barbara" sort="Danneels, Barbara" uniqKey="Danneels B" first="Barbara" last="Danneels">Barbara Danneels</name></region><name sortKey="Desmet, Tom" sort="Desmet, Tom" uniqKey="Desmet T" first="Tom" last="Desmet">Tom Desmet</name><name sortKey="Tanghe, Magali" sort="Tanghe, Magali" uniqKey="Tanghe M" first="Magali" last="Tanghe">Magali Tanghe</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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