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Microbial soluble aromatic prenyltransferases for engineered biosynthesis
Prenyltransferase (PTase) enzymes play crucial roles in natural product biosynthesis by transferring isoprene unit(s) to target substrates, thereby generating prenylated compounds. The prenylation step leads to a diverse group of natural products with improved membrane affinity and enhanced bioactiv...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
KeAi Publishing
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7973389/ https://www.ncbi.nlm.nih.gov/pubmed/33778178 http://dx.doi.org/10.1016/j.synbio.2021.02.001 |
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author | Chen, He-Ping Abe, Ikuro |
author_facet | Chen, He-Ping Abe, Ikuro |
author_sort | Chen, He-Ping |
collection | PubMed |
description | Prenyltransferase (PTase) enzymes play crucial roles in natural product biosynthesis by transferring isoprene unit(s) to target substrates, thereby generating prenylated compounds. The prenylation step leads to a diverse group of natural products with improved membrane affinity and enhanced bioactivity, as compared to the non-prenylated forms. The last two decades have witnessed increasing studies on the identification, characterization, enzyme engineering, and synthetic biology of microbial PTase family enzymes. We herein summarize several examples of microbial soluble aromatic PTases for chemoenzymatic syntheses of unnatural novel prenylated compounds. |
format | Online Article Text |
id | pubmed-7973389 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | KeAi Publishing |
record_format | MEDLINE/PubMed |
spelling | pubmed-79733892021-03-25 Microbial soluble aromatic prenyltransferases for engineered biosynthesis Chen, He-Ping Abe, Ikuro Synth Syst Biotechnol Article Prenyltransferase (PTase) enzymes play crucial roles in natural product biosynthesis by transferring isoprene unit(s) to target substrates, thereby generating prenylated compounds. The prenylation step leads to a diverse group of natural products with improved membrane affinity and enhanced bioactivity, as compared to the non-prenylated forms. The last two decades have witnessed increasing studies on the identification, characterization, enzyme engineering, and synthetic biology of microbial PTase family enzymes. We herein summarize several examples of microbial soluble aromatic PTases for chemoenzymatic syntheses of unnatural novel prenylated compounds. KeAi Publishing 2021-03-15 /pmc/articles/PMC7973389/ /pubmed/33778178 http://dx.doi.org/10.1016/j.synbio.2021.02.001 Text en © 2021 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Article Chen, He-Ping Abe, Ikuro Microbial soluble aromatic prenyltransferases for engineered biosynthesis |
title | Microbial soluble aromatic prenyltransferases for engineered biosynthesis |
title_full | Microbial soluble aromatic prenyltransferases for engineered biosynthesis |
title_fullStr | Microbial soluble aromatic prenyltransferases for engineered biosynthesis |
title_full_unstemmed | Microbial soluble aromatic prenyltransferases for engineered biosynthesis |
title_short | Microbial soluble aromatic prenyltransferases for engineered biosynthesis |
title_sort | microbial soluble aromatic prenyltransferases for engineered biosynthesis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7973389/ https://www.ncbi.nlm.nih.gov/pubmed/33778178 http://dx.doi.org/10.1016/j.synbio.2021.02.001 |
work_keys_str_mv | AT chenheping microbialsolublearomaticprenyltransferasesforengineeredbiosynthesis AT abeikuro microbialsolublearomaticprenyltransferasesforengineeredbiosynthesis |