Cargando…

Identification and investigation of a novel NADP(+)-dependent secoisolariciresinol dehydrogenase from Isatis indigotica

Cofactors are crucial for the biosynthesis of natural compounds, and cofactor engineering is a useful strategy for enzyme optimization due to its potential to enhance enzyme efficiency. Secoisolariciresinol dehydrogenase (SIRD) was reported to convert secoisolariciresinol into matairesinol in an NAD...

Descripción completa

Detalles Bibliográficos
Autores principales: Shi, Xiaoyi, Geng, Jiaran, Feng, Jingxian, Yang, Yingbo, Ma, Xueqi, Chen, Wansheng, Xiao, Ying
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9666873/
https://www.ncbi.nlm.nih.gov/pubmed/36407599
http://dx.doi.org/10.3389/fpls.2022.1035121
_version_ 1784831598277951488
author Shi, Xiaoyi
Geng, Jiaran
Feng, Jingxian
Yang, Yingbo
Ma, Xueqi
Chen, Wansheng
Xiao, Ying
author_facet Shi, Xiaoyi
Geng, Jiaran
Feng, Jingxian
Yang, Yingbo
Ma, Xueqi
Chen, Wansheng
Xiao, Ying
author_sort Shi, Xiaoyi
collection PubMed
description Cofactors are crucial for the biosynthesis of natural compounds, and cofactor engineering is a useful strategy for enzyme optimization due to its potential to enhance enzyme efficiency. Secoisolariciresinol dehydrogenase (SIRD) was reported to convert secoisolariciresinol into matairesinol in an NAD(+)-dependent reaction. Here, a SIRD designated as IiSIRD2 identified from Isatis indigotica was found to utilize NADP(+) as the cofactor. To explore the structural basis for this unique cofactor preference, model-based structural analysis was carried out, and it was postulated that a variation at the GXGGXG glycine-rich motif of IiSIRD2 alters its cofactor preference. This study paves way for future investigations on SIRD cofactor specificity and cofactor engineering to improve SIRD’s catalytic efficiency.
format Online
Article
Text
id pubmed-9666873
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Frontiers Media S.A.
record_format MEDLINE/PubMed
spelling pubmed-96668732022-11-17 Identification and investigation of a novel NADP(+)-dependent secoisolariciresinol dehydrogenase from Isatis indigotica Shi, Xiaoyi Geng, Jiaran Feng, Jingxian Yang, Yingbo Ma, Xueqi Chen, Wansheng Xiao, Ying Front Plant Sci Plant Science Cofactors are crucial for the biosynthesis of natural compounds, and cofactor engineering is a useful strategy for enzyme optimization due to its potential to enhance enzyme efficiency. Secoisolariciresinol dehydrogenase (SIRD) was reported to convert secoisolariciresinol into matairesinol in an NAD(+)-dependent reaction. Here, a SIRD designated as IiSIRD2 identified from Isatis indigotica was found to utilize NADP(+) as the cofactor. To explore the structural basis for this unique cofactor preference, model-based structural analysis was carried out, and it was postulated that a variation at the GXGGXG glycine-rich motif of IiSIRD2 alters its cofactor preference. This study paves way for future investigations on SIRD cofactor specificity and cofactor engineering to improve SIRD’s catalytic efficiency. Frontiers Media S.A. 2022-11-02 /pmc/articles/PMC9666873/ /pubmed/36407599 http://dx.doi.org/10.3389/fpls.2022.1035121 Text en Copyright © 2022 Shi, Geng, Feng, Yang, Ma, Chen and Xiao https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Shi, Xiaoyi
Geng, Jiaran
Feng, Jingxian
Yang, Yingbo
Ma, Xueqi
Chen, Wansheng
Xiao, Ying
Identification and investigation of a novel NADP(+)-dependent secoisolariciresinol dehydrogenase from Isatis indigotica
title Identification and investigation of a novel NADP(+)-dependent secoisolariciresinol dehydrogenase from Isatis indigotica
title_full Identification and investigation of a novel NADP(+)-dependent secoisolariciresinol dehydrogenase from Isatis indigotica
title_fullStr Identification and investigation of a novel NADP(+)-dependent secoisolariciresinol dehydrogenase from Isatis indigotica
title_full_unstemmed Identification and investigation of a novel NADP(+)-dependent secoisolariciresinol dehydrogenase from Isatis indigotica
title_short Identification and investigation of a novel NADP(+)-dependent secoisolariciresinol dehydrogenase from Isatis indigotica
title_sort identification and investigation of a novel nadp(+)-dependent secoisolariciresinol dehydrogenase from isatis indigotica
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9666873/
https://www.ncbi.nlm.nih.gov/pubmed/36407599
http://dx.doi.org/10.3389/fpls.2022.1035121
work_keys_str_mv AT shixiaoyi identificationandinvestigationofanovelnadpdependentsecoisolariciresinoldehydrogenasefromisatisindigotica
AT gengjiaran identificationandinvestigationofanovelnadpdependentsecoisolariciresinoldehydrogenasefromisatisindigotica
AT fengjingxian identificationandinvestigationofanovelnadpdependentsecoisolariciresinoldehydrogenasefromisatisindigotica
AT yangyingbo identificationandinvestigationofanovelnadpdependentsecoisolariciresinoldehydrogenasefromisatisindigotica
AT maxueqi identificationandinvestigationofanovelnadpdependentsecoisolariciresinoldehydrogenasefromisatisindigotica
AT chenwansheng identificationandinvestigationofanovelnadpdependentsecoisolariciresinoldehydrogenasefromisatisindigotica
AT xiaoying identificationandinvestigationofanovelnadpdependentsecoisolariciresinoldehydrogenasefromisatisindigotica