Campus Units

Biochemistry, Biophysics and Molecular Biology

Document Type

Article

Publication Version

Published Version

Publication Date

2007

Journal or Book Title

Journal of the American Chemical Society

Volume

129

Issue

51

First Page

15736

Last Page

15737

DOI

10.1021/ja074977g

Abstract

Terpene synthases often catalyze complex cyclization reactions that typically represent the committed step in particular biosynthetic pathways, leading to great interest in their enzymatic mechanisms. We have recently demonstrated that substitution of a specific Ile with Thr was sufficient to “short circuit” the complex cyclization reaction normally catalyzed by ent-kaurene synthases to instead produce ent-pimaradiene. Here we report that the complex cyclization/rearrangement reaction catalyzed by abietadiene synthase can be similarly cut short to produce pimaradienes by an analogous Ser for Ala change, albeit with a slight shift in active site location to accommodate the difference in substrate stereochemistry. This result has mechanistic implications for enzymatic catalysis of abietadiene cyclization, and terpene synthases more broadly. Furthermore, these defined single residue switches may be useful in engineering product outcome in diterpene synthases more generally.

Comments

This article is published as A Single Residue Switch Converts Abietadiene Synthase into a Pimaradiene Specific Cyclase, P. Ross Wilderman and and Reuben J. Peters, Journal of the American Chemical Society 2007 129 (51), 15736-15737, DOI: 10.1021/ja074977g. This article is made available under ACS AuthorChoice.

Copyright Owner

American Chemical Society

Language

en

File Format

application/pdf

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