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

Chemistry (Twin Cities)

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

11 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 (US)
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 - Feb 2 2018

Bibliographical note

Funding Information:
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).

Publisher Copyright:
© 2017 American Chemical Society.

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10.1021/acscatal.7b02823

http://europepmc.org/articles/pmc5968826

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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.",

author = "Mudit Dixit and Michal Weitman and Jiali Gao and Major, {Dan T.}",

note = "Funding Information: 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). Publisher Copyright: {\textcopyright} 2017 American Chemical Society.",

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doi = "10.1021/acscatal.7b02823",

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T1 - Comment on "substrate Folding Modes in Trichodiene Synthase

T2 - A Determinant of Chemo- and Stereoselectivity"

AU - Dixit, Mudit

AU - Weitman, Michal

AU - Gao, Jiali

AU - Major, Dan T.

N1 - Funding Information: 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). Publisher Copyright: © 2017 American Chemical Society.

PY - 2018/2/2

Y1 - 2018/2/2

N2 - 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.

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

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