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dc.contributor.authorBhan, N.
dc.contributor.authorLi, L.
dc.contributor.authorXu, P.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorKoffas, M.
dc.date2015
dc.date.accessioned2022-06-27T16:05:22Z
dc.date.available2022-06-27T16:05:22Z
dc.date.issued2015
dc.identifier.citationEnzymatic formation of novel resorcylic acid by creating a structure guided single point mutation in stilbene synthase, N. Bhan, L. Li, P. Xu, R. J. Linhardt, M. Koffas, Protein Science, 24,167-173, 2015.
dc.identifier.urihttps://doi.org/10.1002/pro.2600
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5687
dc.descriptionProtein Science, 24,167-173
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractA novel C17 resorcylic acid was synthesized by a structure-guided Vitis vinifera stilbene synthase (STS) mutant, in which threonine 197 was replaced with glycine (T197G). Altering the architecture of the coumaroyl binding and cyclization pocket of the enzyme led to the attachment of an extra acetyl unit, derived from malonyl-CoA, to p-coumaroyl-CoA. The resulting novel pentaketide can be produced strictly by STS-like enzymes and not by Chalcone synthase-like type III polyketide synthases; due to the unique thioesterase like activity of STS-like enzymes. We utilized a liquid chromatography mass spectrometry-based data analysis approach to directly compare the reaction products of the mutant and wild type STS. The findings suggest an easy to employ platform for precursor-directed biosynthesis and identification of unnatural polyketides by structure-guided mutation of STS-like enzymes.
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleEnzymatic formation of novel resorcylic acid by creating a structure guided single point mutation in stilbene synthase
dc.typeArticle
dcterms.isVersionOfhttps://doi.org/10.1002/pro.2600
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)


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