Enzymatic studies on aromatic prenyltransferases

Aromatic prenyltransferases (PTases), including ABBA-type and dimethylallyl tryptophan synthase (DMATS)-type enzymes from bacteria and fungi, play important role for diversification of the natural products and improvement of the biological activities. For a decade, the characterization of enzymes an...

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Autor principal: Mori, Takahiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Singapore 2020
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7253389/
https://www.ncbi.nlm.nih.gov/pubmed/32180104
http://dx.doi.org/10.1007/s11418-020-01393-x
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author Mori, Takahiro
author_facet Mori, Takahiro
author_sort Mori, Takahiro
collection PubMed
description Aromatic prenyltransferases (PTases), including ABBA-type and dimethylallyl tryptophan synthase (DMATS)-type enzymes from bacteria and fungi, play important role for diversification of the natural products and improvement of the biological activities. For a decade, the characterization of enzymes and enzymatic synthesis of prenylated compounds by using ABBA-type and DMATS-type PTases have been demonstrated. Here, I introduce several examples of the studies on chemoenzymatic synthesis of unnatural prenylated compounds and the enzyme engineering of ABBA-type and DMATS-type PTases.
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spelling pubmed-72533892020-06-08 Enzymatic studies on aromatic prenyltransferases Mori, Takahiro J Nat Med Review Aromatic prenyltransferases (PTases), including ABBA-type and dimethylallyl tryptophan synthase (DMATS)-type enzymes from bacteria and fungi, play important role for diversification of the natural products and improvement of the biological activities. For a decade, the characterization of enzymes and enzymatic synthesis of prenylated compounds by using ABBA-type and DMATS-type PTases have been demonstrated. Here, I introduce several examples of the studies on chemoenzymatic synthesis of unnatural prenylated compounds and the enzyme engineering of ABBA-type and DMATS-type PTases. Springer Singapore 2020-03-17 2020 /pmc/articles/PMC7253389/ /pubmed/32180104 http://dx.doi.org/10.1007/s11418-020-01393-x Text en © The Author(s) 2020, corrected publication 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/), which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Review
Mori, Takahiro
Enzymatic studies on aromatic prenyltransferases
title Enzymatic studies on aromatic prenyltransferases
title_full Enzymatic studies on aromatic prenyltransferases
title_fullStr Enzymatic studies on aromatic prenyltransferases
title_full_unstemmed Enzymatic studies on aromatic prenyltransferases
title_short Enzymatic studies on aromatic prenyltransferases
title_sort enzymatic studies on aromatic prenyltransferases
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7253389/
https://www.ncbi.nlm.nih.gov/pubmed/32180104
http://dx.doi.org/10.1007/s11418-020-01393-x
work_keys_str_mv AT moritakahiro enzymaticstudiesonaromaticprenyltransferases

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