Comment on "substrate Folding Modes in Trichodiene Synthase: A Determinant of Chemo- and Stereoselectivity"

Mudit Dixit; Michal Weitman; Jiali Gao; Dan T. Major

doi:10.1021/acscatal.7b02823

Comment on "substrate Folding Modes in Trichodiene Synthase: A Determinant of Chemo- and Stereoselectivity"

Mudit Dixit
, Michal Weitman
, Jiali Gao
, Dan T. Major

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

Abstract

Wang et al. recently reported an in silico study of the trichodiene synthase (TDS) conversion of farnesyl diphosphate (FPP) to trichodiene (TD) (Wang et al., ACS Catal. 2017, 7, 5841-5846). Although the methods and level of theory used in that work are nearly identical to our own recent work on this system (Dixit et al., ACS Catal. 2017, 7, 812-818), Wang et al. reach rather different conclusions. The authors claimed to obtain a "very credible" mechanism for the biosynthesis of TD based on the optimized folding mode of FPP in the 1,6-ring closure in TDS. However, the folding mode of the FPP substrate that was presented contradicts NMR and mass spectrometry data. Moreover, the authors make numerous incorrect statements regarding our earlier work.

Original language	English
Pages (from-to)	1371-1375
Number of pages	5
Journal	ACS Catalysis
Volume	8
Issue number	2
DOIs	https://doi.org/10.1021/acscatal.7b02823
State	Published - 2 Feb 2018

Bibliographical note

Publisher Copyright:
© 2017 American Chemical Society.

Funding

This contribution has been supported by the Israel Science Foundation (Grant No. 2146/15), the National Institutes of Health (GM46736), and National Natural Science Foundation of China (Grant No. 21533003).

Funders	Funder number
National Institutes of Health	GM46736
National Natural Science Foundation of China	21533003
Israel Science Foundation	2146/15

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10.1021/acscatal.7b02823

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title = "Comment on {"}substrate Folding Modes in Trichodiene Synthase: A Determinant of Chemo- and Stereoselectivity{"}",

abstract = "Wang et al. recently reported an in silico study of the trichodiene synthase (TDS) conversion of farnesyl diphosphate (FPP) to trichodiene (TD) (Wang et al., ACS Catal. 2017, 7, 5841-5846). Although the methods and level of theory used in that work are nearly identical to our own recent work on this system (Dixit et al., ACS Catal. 2017, 7, 812-818), Wang et al. reach rather different conclusions. The authors claimed to obtain a {"}very credible{"} mechanism for the biosynthesis of TD based on the optimized folding mode of FPP in the 1,6-ring closure in TDS. However, the folding mode of the FPP substrate that was presented contradicts NMR and mass spectrometry data. Moreover, the authors make numerous incorrect statements regarding our earlier work.",

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AU - Gao, Jiali

AU - Major, Dan T.

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Comment on "substrate Folding Modes in Trichodiene Synthase: A Determinant of Chemo- and Stereoselectivity"

Abstract

Bibliographical note

Funding

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