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Structure-function and engineering of plant UDP-glycosyltransferase
Natural products synthesized by plants have substantial industrial and medicinal values and are therefore attracting increasing interest in various related industries. Among the key enzyme families involved in the biosynthesis of natural products, uridine diphosphate-dependent glycosyltransferases (...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Research Network of Computational and Structural Biotechnology
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10641439/ https://www.ncbi.nlm.nih.gov/pubmed/37965058 http://dx.doi.org/10.1016/j.csbj.2023.10.046 |
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author | Wang, Mengya Ji, Qiushuang Lai, Bin Liu, Yirong Mei, Kunrong |
author_facet | Wang, Mengya Ji, Qiushuang Lai, Bin Liu, Yirong Mei, Kunrong |
author_sort | Wang, Mengya |
collection | PubMed |
description | Natural products synthesized by plants have substantial industrial and medicinal values and are therefore attracting increasing interest in various related industries. Among the key enzyme families involved in the biosynthesis of natural products, uridine diphosphate-dependent glycosyltransferases (UGTs) play a crucial role in plants. In recent years, significant efforts have been made to elucidate the catalytic mechanisms and substrate recognition of plant UGTs and to improve them for desired functions. In this review, we presented a comprehensive overview of all currently published structures of plant UGTs, along with in-depth analyses of the corresponding catalytic and substrate recognition mechanisms. In addition, we summarized and evaluated the protein engineering strategies applied to improve the catalytic activities of plant UGTs, with a particular focus on high-throughput screening methods. The primary objective of this review is to provide readers with a comprehensive understanding of plant UGTs and to serve as a valuable reference for the latest techniques used to improve their activities. |
format | Online Article Text |
id | pubmed-10641439 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Research Network of Computational and Structural Biotechnology |
record_format | MEDLINE/PubMed |
spelling | pubmed-106414392023-11-14 Structure-function and engineering of plant UDP-glycosyltransferase Wang, Mengya Ji, Qiushuang Lai, Bin Liu, Yirong Mei, Kunrong Comput Struct Biotechnol J Review Article Natural products synthesized by plants have substantial industrial and medicinal values and are therefore attracting increasing interest in various related industries. Among the key enzyme families involved in the biosynthesis of natural products, uridine diphosphate-dependent glycosyltransferases (UGTs) play a crucial role in plants. In recent years, significant efforts have been made to elucidate the catalytic mechanisms and substrate recognition of plant UGTs and to improve them for desired functions. In this review, we presented a comprehensive overview of all currently published structures of plant UGTs, along with in-depth analyses of the corresponding catalytic and substrate recognition mechanisms. In addition, we summarized and evaluated the protein engineering strategies applied to improve the catalytic activities of plant UGTs, with a particular focus on high-throughput screening methods. The primary objective of this review is to provide readers with a comprehensive understanding of plant UGTs and to serve as a valuable reference for the latest techniques used to improve their activities. Research Network of Computational and Structural Biotechnology 2023-10-27 /pmc/articles/PMC10641439/ /pubmed/37965058 http://dx.doi.org/10.1016/j.csbj.2023.10.046 Text en © 2023 The Authors https://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 | Review Article Wang, Mengya Ji, Qiushuang Lai, Bin Liu, Yirong Mei, Kunrong Structure-function and engineering of plant UDP-glycosyltransferase |
title | Structure-function and engineering of plant UDP-glycosyltransferase |
title_full | Structure-function and engineering of plant UDP-glycosyltransferase |
title_fullStr | Structure-function and engineering of plant UDP-glycosyltransferase |
title_full_unstemmed | Structure-function and engineering of plant UDP-glycosyltransferase |
title_short | Structure-function and engineering of plant UDP-glycosyltransferase |
title_sort | structure-function and engineering of plant udp-glycosyltransferase |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10641439/ https://www.ncbi.nlm.nih.gov/pubmed/37965058 http://dx.doi.org/10.1016/j.csbj.2023.10.046 |
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