Enzymatic formation of novel resorcylic acid by creating a structure guided single point mutation in stilbene synthase

Authors
Bhan, N.
Li, L.
Xu, P.
Linhardt, Robert J.
Koffas, M.
ORCID
https://orcid.org/0000-0003-2219-5833
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Other Contributors
Issue Date
2015
Keywords
Biology , Chemistry and chemical biology , Chemical and biological engineering , Biomedical engineering
Degree
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Full Citation
Enzymatic 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.
Abstract
A 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.
Description
Protein Science, 24,167-173
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Department
The Linhardt Research Labs.
The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
Publisher
Relationships
The Linhardt Research Labs Online Collection
Rensselaer Polytechnic Institute, Troy, NY
https://harc.rpi.edu/
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