Shi Xiaoyi, Geng Jiaran, Feng Jingxian, Yang Yingbo, Ma Xueqi, Chen Wansheng, Xiao Ying
Research and Development Center of Chinese Medicine Resources and Biotechnology, The Ministry of Education (MOE) Key Laboratory for Standardization of Chinese Medicines, Institute of Chinese Materia Medica, Shanghai University of Traditional Chinese Medicine, Shanghai, China.
Shanghai Foreign Language School Affiliated to Shanghai International Studies University (SISU), Shanghai, China.
Front Plant Sci. 2022 Nov 2;13:1035121. doi: 10.3389/fpls.2022.1035121. eCollection 2022.
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 SIRD2 identified from 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 SIRD2 alters its cofactor preference. This study paves way for future investigations on SIRD cofactor specificity and cofactor engineering to improve SIRD's catalytic efficiency.
辅因子对于天然化合物的生物合成至关重要，并且由于其具有提高酶效率的潜力，辅因子工程是一种用于酶优化的有用策略。据报道，开环异落叶松脂醇脱氢酶（SIRD）在依赖NAD的反应中将开环异落叶松脂醇转化为罗汉松脂醇。在此，从[具体来源未给出]中鉴定出的一种名为SIRD2的SIRD被发现利用NADP作为辅因子。为了探究这种独特辅因子偏好的结构基础，进行了基于模型的结构分析，并推测SIRD2富含甘氨酸的GXGGXG基序处的变异改变了其辅因子偏好。该研究为未来关于SIRD辅因子特异性以及通过辅因子工程提高SIRD催化效率的研究铺平了道路。
