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


ABSTRACT: 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.

SUBMITTER: Shi X 

PROVIDER: S-EPMC9666873 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature

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Identification and investigation of a novel NADP<sup>+</sup>-dependent secoisolariciresinol dehydrogenase from <i>Isatis indigotica</i>.

Shi Xiaoyi X   Geng Jiaran J   Feng Jingxian J   Yang Yingbo Y   Ma Xueqi X   Chen Wansheng W   Xiao Ying Y  

Frontiers in plant science 20221102


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<sup>+</sup>-dependent reaction. Here, a SIRD designated as <i>Ii</i>SIRD2 identified from <i>Isatis indigotica</i> was found to utilize NADP<sup>+</sup> as the cofactor. To explore the structural bas  ...[more]

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