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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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Autores principales: Gu, Binbin, Liang, Lin-Fu, Dickschat, Jeroen S
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Beilstein-Institut 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10520479/
https://www.ncbi.nlm.nih.gov/pubmed/37767334
http://dx.doi.org/10.3762/bjoc.19.104
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author Gu, Binbin
Liang, Lin-Fu
Dickschat, Jeroen S
author_facet Gu, Binbin
Liang, Lin-Fu
Dickschat, Jeroen S
author_sort Gu, Binbin
collection PubMed
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 C(12) monoterpenoids. Implications on the stereochemical course of the terpene cyclisation by 2-methylisoborneol synthase are discussed.
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spelling pubmed-105204792023-09-27 Functions of enzyme domains in 2-methylisoborneol biosynthesis and enzymatic synthesis of non-natural analogs Gu, Binbin Liang, Lin-Fu Dickschat, Jeroen S Beilstein J Org Chem Letter 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 C(12) monoterpenoids. Implications on the stereochemical course of the terpene cyclisation by 2-methylisoborneol synthase are discussed. Beilstein-Institut 2023-09-22 /pmc/articles/PMC10520479/ /pubmed/37767334 http://dx.doi.org/10.3762/bjoc.19.104 Text en Copyright © 2023, Gu et al. https://creativecommons.org/licenses/by/4.0/This is an open access article licensed under the terms of the Beilstein-Institut Open Access License Agreement (https://www.beilstein-journals.org/bjoc/terms/terms), which is identical to the Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0 (https://creativecommons.org/licenses/by/4.0/) ). The reuse of material under this license requires that the author(s), source and license are credited. Third-party material in this article could be subject to other licenses (typically indicated in the credit line), and in this case, users are required to obtain permission from the license holder to reuse the material.
spellingShingle Letter
Gu, Binbin
Liang, Lin-Fu
Dickschat, Jeroen S
Functions of enzyme domains in 2-methylisoborneol biosynthesis and enzymatic synthesis of non-natural analogs
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 Letter
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10520479/
https://www.ncbi.nlm.nih.gov/pubmed/37767334
http://dx.doi.org/10.3762/bjoc.19.104
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