Elucidating Sequence and Structural Determinants of Carbohydrate Esterases for Complete Deacetylation of Substituted Xylans

dc.contributorAalto-yliopistofi
dc.contributorAalto Universityen
dc.contributor.authorPenttinen, Leenaen_US
dc.contributor.authorKouhi, Veraen_US
dc.contributor.authorFauré, Régisen_US
dc.contributor.authorSkarina, Tatianaen_US
dc.contributor.authorStogios, Peteren_US
dc.contributor.authorMaster, Emmaen_US
dc.contributor.authorJurak, Editaen_US
dc.contributor.departmentDepartment of Bioproducts and Biosystemsen
dc.contributor.groupauthorProtein Technologyen
dc.contributor.organizationUniversity of Helsinkien_US
dc.contributor.organizationLaboratoire d'Ingénierie des Systèmes Biologiques et des Procédésen_US
dc.contributor.organizationUniversity of Torontoen_US
dc.contributor.organizationUniversity of Eastern Finlanden_US
dc.contributor.organizationUniversity of Groningenen_US
dc.date.accessioned2022-06-08T06:12:06Z
dc.date.available2022-06-08T06:12:06Z
dc.date.issued2022-05-01en_US
dc.description| openaire: EC/H2020/648925/EU//BHIVE
dc.description.abstractAcetylated glucuronoxylan is one of the most common types of hemicellulose in nature. The structure is formed by a β-(1→4)-linked D-xylopyranosyl (Xylp) backbone that can be substituted with an acetyl group at O-2 and O-3 positions, and α-(1→2)-linked 4-O-methylglucopyranosyluronic acid (MeGlcpA). Acetyl xylan esterases (AcXE) that target mono-or doubly acetylated Xylp are well characterized; however, the previously studied AcXE from Flavobacterium johnsoniae (FjoAcXE) was the first to remove the acetyl group from 2-O-MeGlcpA-3-O-acetyl-substituted Xylp units, yet structural characteristics of these enzymes remain unspecified. Here, six homologs of FjoAcXE were produced and three crystal structures of the enzymes were solved. Two of them are complex structures, one with bound MeGlcpA and another with acetate. All homologs were confirmed to release acetate from 2-O-MeGlcpA-3-O-acetyl-substituted xylan, and the crystal structures point to key structural elements that might serve as defining features of this unclassified carbohydrate esterase family. Enzymes comprised two domains: N-terminal CBM domain and a C-terminal SGNH domain. In FjoAcXE and all studied homologs, the sequence motif around the catalytic serine is Gly-Asn-Ser-Ile (GNSI), which differs from other SGNH hydrolases. Binding by the MeGlcpA-Xylp ligand is directed by positively charged and highly conserved residues at the interface of the CBM and SGNH domains of the enzyme.en
dc.description.versionPeer revieweden
dc.format.extent15
dc.format.mimetypeapplication/pdfen_US
dc.identifier.citationPenttinen, L, Kouhi, V, Fauré, R, Skarina, T, Stogios, P, Master, E & Jurak, E 2022, ' Elucidating Sequence and Structural Determinants of Carbohydrate Esterases for Complete Deacetylation of Substituted Xylans ', Molecules, vol. 27, no. 9, 2655 . https://doi.org/10.3390/molecules27092655en
dc.identifier.doi10.3390/molecules27092655en_US
dc.identifier.issn1420-3049
dc.identifier.otherPURE UUID: 4f58f1b0-fe0c-49ec-848c-963ee8aec709en_US
dc.identifier.otherPURE ITEMURL: https://research.aalto.fi/en/publications/4f58f1b0-fe0c-49ec-848c-963ee8aec709en_US
dc.identifier.otherPURE LINK: http://www.scopus.com/inward/record.url?scp=85129286615&partnerID=8YFLogxKen_US
dc.identifier.otherPURE FILEURL: https://research.aalto.fi/files/83411502/CHEM_Penttinen_et_al_Elucidating_Sequence_2022_Molecules.pdfen_US
dc.identifier.urihttps://aaltodoc.aalto.fi/handle/123456789/114762
dc.identifier.urnURN:NBN:fi:aalto-202206083605
dc.language.isoenen
dc.publisherMDPI AG
dc.relationinfo:eu-repo/grantAgreement/EC/H2020/648925/EU//BHIVEen_US
dc.relation.ispartofseriesMoleculesen
dc.relation.ispartofseriesVolume 27, issue 9en
dc.rightsopenAccessen
dc.subject.keywordacetyl xylan esteraseen_US
dc.subject.keywordcarbohydrate esteraseen_US
dc.subject.keywordSGNH hydrolaseen_US
dc.subject.keywordxylanen_US
dc.titleElucidating Sequence and Structural Determinants of Carbohydrate Esterases for Complete Deacetylation of Substituted Xylansen
dc.typeA1 Alkuperäisartikkeli tieteellisessä aikakauslehdessäfi
dc.type.versionpublishedVersion

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