Effects of Substrate-Binding Site Residues on the Biochemical Properties of a Tau Class Glutathione S-Transferase from Oryza sativa
文献类型：期刊论文
| 作者 | Yang, Xue4; Wei, Jinchi3; Wu, Zhihai5; Gao, Jie1,2 |
| 刊名 | GENES
 |
| 出版日期 | 2020 |
| 卷号 | 11期号:1 |
| 关键词 | glutathione S-transferase glutathione-binding site hydrophobic substrate-binding site site-directed mutagenesis enzymatic properties |
| DOI | 10.3390/genes11010025 |
| 文献子类 | Article |
| 英文摘要 | Glutathione S-transferases (GSTs)-an especially plant-specific tau class of GSTs-are key enzymes involved in biotic and abiotic stress responses. To improve the stress resistance of crops via the genetic modification of GSTs, we predicted the amino acids present in the GSH binding site (G-site) and hydrophobic substrate-binding site (H-site) of OsGSTU17, a tau class GST in rice. We then examined the enzyme activity, substrate specificity, enzyme kinetics and thermodynamic stability of the mutant enzymes. Our results showed that the hydrogen bonds between Lys42, Val56, Glu68, and Ser69 of the G-site and glutathione were essential for enzyme activity and thermal stability. The hydrophobic side chains of amino acids of the H-site contributed to enzyme activity toward 4-nitrobenzyl chloride but had an inhibitory effect on enzyme activity toward 1-chloro-2,4-dinitrobenzene and cumene hydroperoxide. Different amino acids of the H-site had different effects on enzyme activity toward a different substrate, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Moreover, Leu112 and Phe162 were found to inhibit the catalytic efficiency of OsGSTU17 to 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, while Pro16, Leu112, and Trp165 contributed to structural stability. The results of this research enhance the understanding of the relationship between the structure and function of tau class GSTs to improve the abiotic stress resistance of crops. |
| 学科主题 | Genetics & Heredity |
| 出版地 | BASEL |
| 电子版国际标准刊号 | 2073-4425 |
| WOS关键词 | SUPERGENE FAMILY ; CATALYTIC MECHANISM ; GENE FAMILY ; EVOLUTION ; TOLERANCE ; EXPRESSION ; FLUORODIFEN ; DIVERGENCE ; REVEALS ; DROUGHT |
| WOS研究方向 | Genetics & Heredity |
| 语种 | 英语 |
| WOS记录号 | WOS:000514898000025 |
| 出版者 | MDPI |
| 资助机构 | National Key R&D Program of the Ministry of Agriculture and Rural Affairs of the People's Republic of China [2017YFD0300609] ; Science and Technology Research Project of Department of Education of Jilin Provincial [JJKH20180656KJ] |
| 源URL | [http://ir.ibcas.ac.cn/handle/2S10CLM1/21898]  |
| 专题 | 植物研究所_系统与进化植物学研究中心_系统与进化植物学研究中心_学位论文 |
| 作者单位 | 1.Chinese Acad Sci, Xishuangbanna Trop Bot Garden, CAS Key Lab Trop Forest Ecol, Menglun 666303, Peoples R China 2.Jilin Agr Univ, Fac Agron, Changchun 130118, Peoples R China 3.Chinese Acad Sci, Inst Bot, State Key Lab Systemat & Evolutionary Bot, Beijing 100093, Peoples R China 4.Jilin Agr Univ, Coll Life Sci, Changchun 130118, Peoples R China 5.Beijing Forestry Univ, Coll Biol Sci & Technol, Beijing 100083, Peoples R China 6.Chinese Acad Sci, Core Bot Gardens, Ctr Conservat Biol, Mengla 666303, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yang, Xue,Wei, Jinchi,Wu, Zhihai,et al. Effects of Substrate-Binding Site Residues on the Biochemical Properties of a Tau Class Glutathione S-Transferase from Oryza sativa[J]. GENES,2020,11(1). |
| APA | Yang, Xue,Wei, Jinchi,Wu, Zhihai,&Gao, Jie.(2020).Effects of Substrate-Binding Site Residues on the Biochemical Properties of a Tau Class Glutathione S-Transferase from Oryza sativa.GENES,11(1). |
| MLA | Yang, Xue,et al."Effects of Substrate-Binding Site Residues on the Biochemical Properties of a Tau Class Glutathione S-Transferase from Oryza sativa".GENES 11.1(2020). |
入库方式： OAI收割
来源：植物研究所
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