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Issue 5, 2019
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Silent catalytic promiscuity in the high-fidelity terpene cyclase δ-cadinene synthase

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Abstract

δ-Cadinene synthase (DCS) is a high-fidelity sesquiterpene synthase that generates δ-cadinene as the sole detectable organic product from its natural substrate (E,E)-FDP. Previous work with this enzyme using substrate analogues revealed the ability of DCS to catalyse both 1,10- and 1,6-cyclisations of substrate analogues. To test whether this apparent promiscuity was an artefact of alternate substrate use or an inherent property of the enzyme, aza analogues of the proposed α-bisabolyl cation intermediate were prepared since this cation would be formed after an initial 1,6-cyclisation of FDP. In the presence of 250 μM inorganic disphosphate both (R)- and (S)-aza-bisaboyl cations were potent competitive inhibitors of DCS (Ki = 2.5 ± 0.5 mM and 3.44 ± 1.43 μM, respectively). These compounds were also shown to be potent inhibitors of the 1,6-cyclase amorpha-4,11-diene synthase but not of the 1,10-cyclase aristolochene synthase from Penicillium roquefortii, demonstrating that the 1,6-cyclase activity of DCS is most likely an inherent property of the enzyme even when the natural substrate is used and not an artefact of the use of substrate analogues.

Graphical abstract: Silent catalytic promiscuity in the high-fidelity terpene cyclase δ-cadinene synthase

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Publication details

The article was received on 13 Nov 2018, accepted on 10 Dec 2018 and first published on 17 Jan 2019


Article type: Paper
DOI: 10.1039/C8OB02821D
Citation: Org. Biomol. Chem., 2019,17, 1206-1214
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    Silent catalytic promiscuity in the high-fidelity terpene cyclase δ-cadinene synthase

    M. Loizzi, D. J. Miller and R. K. Allemann, Org. Biomol. Chem., 2019, 17, 1206
    DOI: 10.1039/C8OB02821D

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