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. 2016 May 10;7:638. doi: 10.3389/fpls.2016.00638

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Copyright © 2016 Ruan, Li, Fang, Wang, Hu, Chen and Yang.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Enzymatic characterization of AaTPS2, AaTPS5, and AaTPS6 recombinant proteins. (A) GC–MS analysis of pentane extracts of AaTPS6, AaTPS2, and AaTPS5 recombinant proteins after incubation with GPP as substrate. The protein tag produced by pET32a empty vector was used as control. (B,C) Product percentages of AaTPS5 (B) and AaTPS6 (C), sabinene (peaks 5) and β-phellandrene (peak 7) were calculated together because they could not be separated well by gas chromatography. Peaks are: (1) tricyclene; (2) α-thujene; (3) α-pinene; (4) camphene; (5) sabinene; (6) β-pinene; (7) β-phellandrene; (8) β-myrcene; (9) 1,8-cineole; (10) trans-sabinene hydrate; (11) cis-β-terpineol; (13) α-terpineol; (12) and (14) products unidentified. (D) Relative activities of AaTPS2, AaTPS5, and AaTPS6 with different divalent metal cofactors. (E) Relative activities of AaTPS2, AaTPS5, and AaTPS6 recombinant proteins toward GPP substrate at different temperatures.