Study on a Mechanism of Improving MaAPX1 Protein Activity by Mutating Methionine to Lysine
文献类型： 外文期刊
作者： Xiao, Lu 1 ; Jiang, Guoxiang 1 ; Lai, Hongmei 1 ; Duan, Xiaoyan 1 ; Yan, Huiling 3 ; Chen, Shaoge 1 ; Chen, Zexin 4 ; Duan, Xuewu 1 ;
作者机构： 1.Chinese Acad Sci, Guangdong Prov Key Lab Appl Bot, South China Bot Garden, Guangzhou 510650, Peoples R China
2.Guangdong Acad Agr Sci, Inst Qual Stand & Monitoring Technol Agroprod, Guangzhou 510640, Peoples R China
3.Chengdu Univ, Sch Food & Biol Engn, Chengdu 610106, Peoples R China
4.Accurate Int Biotechnol Co Ltd, Guangzhou 510535, Peoples R China
关键词： ascorbate peroxidase 1 (APX1); activity; S-nitrosylation; enzyme kinetics; molecular docking
期刊名称：ANTIOXIDANTS （ 影响因子：6.0； 五年影响因子：6.7 ）
ISSN：
年卷期： 2024 年 13 卷 7 期
页码：
收录情况： SCI
摘要： Ascorbate peroxidases (APXs) are key components of the ascorbate-glytathione cycle, which plays an important role in removing excess reactive oxygen species (ROS) in plants. Herein, MaAPX1 was verified as being involved in the ripening and senescence of banana fruit, exhibiting responsiveness to the accumulation of ROS and the oxidation of proteins. Site-directed mutation was applied to explore the mechanism of MaAPX1 activity changes. We found that the 32-site cysteine (Cys, C) served as a potential S-nitrosylation site. The mutant MaAPX1C32S activity was decreased significantly when Cys32 was mutated to serine (Ser, S). Intriguingly, the neighboring conserved 36-site methionine (Met, M), which is adjacent to Cys32, displayed an enzyme activity that was approximately five times higher than that of the wild-type MaAPX1 when mutated to lysine (Lys, K). Utilizing LC-MS/MS spectroscopy coupled with stopped-flow analysis showed that the enhanced MaAPX1M36K activity might be due to the increased S-nitrosylation level of Cys32 and the promotion of intermediate (compound I, the first intermediate product of the reaction of APX with H2O2) production. Molecular docking simulations showed that the S-N bond between Cys32 and Lys36 in MaAPX1M36K might have a function in protecting the thiol of Cys32 from oxidation. MaAPX1M36K, a promising mutant, possesses immense potential for improving the antioxidant capabilities of APX in the realm of bioengineering technology research.
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