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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...

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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
Descripción
Sumario: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.