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.

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.

Copyright Owner

American Chemical Society

Language

en

File Format

application/pdf

Published Version

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