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dc.contributor.authorChekan, Jonathan R-
dc.contributor.authorMcKinnie, Shaun M. K-
dc.date.accessioned2024-04-19T08:39:48Z-
dc.date.available2024-04-19T08:39:48Z-
dc.date.issued2020-
dc.identifier.otherOER000000769vi
dc.identifier.urihttp://dlib.hust.edu.vn/handle/HUST/24496-
dc.descriptionTài liệu này được phát hành theo giấy phép CC-BY-NC-ND 4.0vi
dc.description.abstractDomoic acid is a neurotoxin produced by marine algae that readily bioaccumulates in shellfish and significantly impacts both human and animal life. The first committed step of the biosynthesis of domoic acid is the N-prenylation of L-glutamic acid by the enzyme DabA. By solving the crystal structure of DabA, we demonstrate that this enzyme has repurposed the common terpene cyclase fold to catalyze an extremely unusual reaction, N-prenylation of an unactivated primary amine. Application of these structural insights enabled rational engineering of two N-prenyltransferase enzymes to accept alternative prenyl donors. Ultimately, these results not only expand the scope of reactions catalyzed by a terpene cyclase family member, but will help inform future domoic acid environmental monitoring efforts.vi
dc.description.urihttps://www.biorxiv.org/content/10.1101/2020.03.31.014811v1vi
dc.formatPDFvi
dc.language.isoenvi
dc.publisherBiochemical Journalvi
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Vietnam*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/vn/*
dc.subjectX-ray crystalvi
dc.subjectDabAvi
dc.subject.lccQD405vi
dc.titleAlgal Neurotoxin Biosynthesis Repurposes the Terpene Cyclase Structural Fold Into an N-prenyltransferasevi
dc.typeJournal articlevi
Appears in Collections:OER - Kỹ thuật cơ khí; Cơ khí động lực; Hàng không; Chế tạo máy

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