Campus Units
Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of
Document Type
Article
Publication Version
Accepted Manuscript
Publication Date
3-8-2018
Journal or Book Title
ACS Catalysis
Volume
8
Issue
4
First Page
3133
Last Page
3137
DOI
10.1021/acscatal.8b00121
Abstract
Sclareol synthase from Salvia sclarea (SsSS) naturally acts on 8α-hydroxy-copalyl diphosphate (1), stereoselectively adding water to produce (13R)-sclareol (2a), and similarly yields hydroxylated products with manifold other such bicyclic diterpene precursors. Here a key residue for this addition of water was identified. Strikingly, substitution with glutamine switches stereochemical outcome with 1, leading to selective production of (13S)-sclareol (2b). Moreover, changes to the stereospecificity of water addition with the structurally closely-related substrate copalyl diphosphate (4) could be accomplished with alternative substitutions. Thus, this approach is expected to provide biosynthetic access to both epimers of 13-hydroxylated derivatives of manifold labdane-related diterpenes.
Copyright Owner
American Chemical Society
Copyright Date
2018
Language
en
File Format
application/pdf
Recommended Citation
Jia, Meirong; O'Brien, Terrence E.; Zhang, Yue; Siegel, Justin B.; Tantillo, Dean J.; and Peters, Reuben J., "Changing Face: A Key Residue for the Addition of Water by Sclareol Synthase" (2018). Biochemistry, Biophysics and Molecular Biology Publications. 265.
https://lib.dr.iastate.edu/bbmb_ag_pubs/265
Included in
Biochemistry Commons, Biophysics Commons, Molecular Biology Commons, Structural Biology Commons
Comments
This is a manuscript of an article published as Jia, Meirong, Terrence E. O’Brien, Yue Zhang, Justin B. Siegel, Dean J. Tantillo, and Reuben J. Peters. "Changing face: a key residue for the addition of water by sclareol synthase." ACS catalysis 8, no. 4 (2018): 3133-3137. doi: 10.1021/acscatal.8b00121. Posted with permission.