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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,...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Beilstein-Institut
2023
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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. |
format | Online Article Text |
id | pubmed-10520479 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Beilstein-Institut |
record_format | MEDLINE/PubMed |
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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