Identification of the Catalytic Residues in the Cyclase Domain of the Class IV Lanthipeptide Synthetase SgbL

dc.contributor.authorHegemann, Julian D.
dc.contributor.authorSüssmuth, Roderich D.
dc.date.accessioned2023-09-08T16:22:14Z
dc.date.available2023-09-08T16:22:14Z
dc.date.issued2021-09-12
dc.description.abstractLanthipeptides belong to the family of ribosomally synthesized and post-translationally modified peptides (RiPPs) and are subdivided into different classes based on their processing enzymes. The three-domain class IV lanthipeptide synthetases (LanL enzymes) consist of N-terminal lyase, central kinase, and C-terminal cyclase domains. While the catalytic residues of the kinase domains (mediating ATP-dependent Ser/Thr phosphorylations) and the lyase domains (carrying out subsequent phosphoserine/phosphothreonine (pSer/pThr) eliminations to yield dehydroalanine/dehydrobutyrine (Dha/Dhb) residues) have been characterized previously, such studies are missing for LanL cyclase domains. To close this gap of knowledge, this study reports on the identification and validation of the catalytic residues in the cyclase domain of the class IV lanthipeptide synthetase SgbL, which facilitate the nucleophilic attacks by Cys thiols on Dha/Dhb residues for the formation of β-thioether crosslinks.en
dc.description.sponsorshipTU Berlin, Open-Access-Mittel – 2021
dc.identifier.eissn1439-7633
dc.identifier.issn1439-4227
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/19995
dc.identifier.urihttps://doi.org/10.14279/depositonce-18793
dc.language.isoen
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.ddc500 Naturwissenschaften und Mathematik::540 Chemie::540 Chemie und zugeordnete Wissenschaften
dc.subject.otherbiocatalysisen
dc.subject.otherbiosynthesisen
dc.subject.otherlanthipeptidesen
dc.subject.othernatural productsen
dc.subject.otherRiPPsen
dc.titleIdentification of the Catalytic Residues in the Cyclase Domain of the Class IV Lanthipeptide Synthetase SgbL
dc.typeArticle
dc.type.versionpublishedVersion
dcterms.bibliographicCitation.doi10.1002/cbic.202100391
dcterms.bibliographicCitation.issue22
dcterms.bibliographicCitation.journaltitleChemBioChem
dcterms.bibliographicCitation.originalpublishernameWiley-VCH
dcterms.bibliographicCitation.originalpublisherplaceWeinheim
dcterms.bibliographicCitation.pageend3172
dcterms.bibliographicCitation.pagestart3169
dcterms.bibliographicCitation.volume22
dcterms.rightsHolder.referenceCreative-Commons-Lizenz
tub.accessrights.dnbfree
tub.affiliationFak. 2 Mathematik und Naturwissenschaften::Inst. Chemie::FG Biologische Chemie
tub.publisher.universityorinstitutionTechnische Universität Berlin

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