Plant terpene synthases are a large class of structurally conserved yet functionally diverse enzymes, which are responsible for making a vast number of terpene compounds. In this study, computational tools were utilized to shed light on the impact of mutations on enzyme dynamics and product profiles. Specifically, domain-swapped terpene synthases with modified functionalities were modeled and simulated with molecular dynamics. Simulations were carried out on several enzyme variants in the presence of a chemical intermediate. Interestingly, our computational studies show a switch of preference in terms of molecular conformations for the chemical intermediate, which is consistent with the change in enzyme product profile as characterized using in vivo assays. In addition, mutational effects on enzyme dynamics in its 3D (eg apo and holo form<b>)</b> were studied at different temperatures.<br/>

Computational investigation of mutational impact on terpene synthases

251st National Meeting (2016)

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