Functions of enzyme domains in 2-methylisoborneol biosynthesis and enzymatic synthesis of non-natural analogs

Two aspects of the biosynthesis of the non-canonical terpene synthase for 2-methylisoborneol have been studied. Several 2-methylisoborneol synthases have a proline-rich N-terminal domain of unknown function. The results presented here demonstrate that this domain leads to a reduced enzyme activity,...

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Main Authors: Binbin Gu, Lin-Fu Liang, Jeroen S. Dickschat
Format: Article
Language:English
Published: Beilstein-Institut 2023-09-01
Series:Beilstein Journal of Organic Chemistry
Subjects:
Online Access:https://doi.org/10.3762/bjoc.19.104
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author Binbin Gu
Lin-Fu Liang
Jeroen S. Dickschat
author_facet Binbin Gu
Lin-Fu Liang
Jeroen S. Dickschat
author_sort Binbin Gu
collection DOAJ
description Two aspects of the biosynthesis of the non-canonical terpene synthase for 2-methylisoborneol have been studied. Several 2-methylisoborneol synthases have a proline-rich N-terminal domain of unknown function. The results presented here demonstrate that this domain leads to a reduced enzyme activity, in addition to its ability to increase long-term solubility of the protein. Furthermore, the substrate scope of the 2-methylisoborneol synthase was investigated through enzyme incubations with several substrate analogs, giving access to two C12 monoterpenoids. Implications on the stereochemical course of the terpene cyclisation by 2-methylisoborneol synthase are discussed.
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spelling doaj.art-80e9e47c54e24626a27f0919eaeb19e12023-10-02T08:42:12ZengBeilstein-InstitutBeilstein Journal of Organic Chemistry1860-53972023-09-011911452145910.3762/bjoc.19.1041860-5397-19-104Functions of enzyme domains in 2-methylisoborneol biosynthesis and enzymatic synthesis of non-natural analogsBinbin Gu0Lin-Fu Liang1Jeroen S. Dickschat2Kekulé-Institute of Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Straße 1, 53121 Bonn, Germany Kekulé-Institute of Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Straße 1, 53121 Bonn, Germany Kekulé-Institute of Organic Chemistry and Biochemistry, University of Bonn, Gerhard-Domagk-Straße 1, 53121 Bonn, Germany Two aspects of the biosynthesis of the non-canonical terpene synthase for 2-methylisoborneol have been studied. Several 2-methylisoborneol synthases have a proline-rich N-terminal domain of unknown function. The results presented here demonstrate that this domain leads to a reduced enzyme activity, in addition to its ability to increase long-term solubility of the protein. Furthermore, the substrate scope of the 2-methylisoborneol synthase was investigated through enzyme incubations with several substrate analogs, giving access to two C12 monoterpenoids. Implications on the stereochemical course of the terpene cyclisation by 2-methylisoborneol synthase are discussed.https://doi.org/10.3762/bjoc.19.104biosynthesisenzymesisotopessubstrate analogsterpenes
spellingShingle Binbin Gu
Lin-Fu Liang
Jeroen S. Dickschat
Functions of enzyme domains in 2-methylisoborneol biosynthesis and enzymatic synthesis of non-natural analogs
Beilstein Journal of Organic Chemistry
biosynthesis
enzymes
isotopes
substrate analogs
terpenes
title Functions of enzyme domains in 2-methylisoborneol biosynthesis and enzymatic synthesis of non-natural analogs
title_full Functions of enzyme domains in 2-methylisoborneol biosynthesis and enzymatic synthesis of non-natural analogs
title_fullStr Functions of enzyme domains in 2-methylisoborneol biosynthesis and enzymatic synthesis of non-natural analogs
title_full_unstemmed Functions of enzyme domains in 2-methylisoborneol biosynthesis and enzymatic synthesis of non-natural analogs
title_short Functions of enzyme domains in 2-methylisoborneol biosynthesis and enzymatic synthesis of non-natural analogs
title_sort functions of enzyme domains in 2 methylisoborneol biosynthesis and enzymatic synthesis of non natural analogs
topic biosynthesis
enzymes
isotopes
substrate analogs
terpenes
url https://doi.org/10.3762/bjoc.19.104
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AT jeroensdickschat functionsofenzymedomainsin2methylisoborneolbiosynthesisandenzymaticsynthesisofnonnaturalanalogs