Trehalose-6-phosphate phosphatase expression and enzymatic properties of Fusarium graminearum
文献类型： 外文期刊
作者： Zhang, Xuebiao 1 ; Chen, Le 2 ; Ni, Zhong 1 ; Xu, Chao 3 ; Wu, Qinyan 3 ; Zhuang, Yiqing 2 ;
作者机构： 1.Jiangsu Univ, Sch Life Sci, Zhenjiang 212000, Jiangsu, Peoples R China
2.Jiangsu Acad Agr Sci, Nanjing 210014, Jiangsu, Peoples R China
3.Zhenjiang Inst Agr Sci Jiangsu Hill Reg, Jurong 212400, Jiangsu, Peoples R China
关键词： Trehalose-6-phosphate; Trehalose-6-phosphate phosphatase; Heterologous expression; Fusarium graminearum
期刊名称：PROTEIN EXPRESSION AND PURIFICATION （ 影响因子：1.2； 五年影响因子：1.6 ）
ISSN： 1046-5928
年卷期： 2025 年 226 卷
页码：
收录情况： SCI
摘要： This study presents an exhaustive characterization of the enzymatic attributes and structural properties of trehalose-6-phosphate phosphatase (TPP) derived from Fusarium graminearum. Enzyme activity was evaluated through a meticulously designed enzymatic assay. The findings indicate that the molecular weight of the enzyme is approximately 99.8 kDa, with an optimal reaction temperature and pH of 40 degrees C and 6.5, respectively. Magnesium ions (Mg2+) markedly enhance the enzymatic activity, resulting in a specific activity of 1.795 U/mu g. Kinetic analysis revealed a Km value of 0.96 mu mol/L and a Vmax of 15.79 mu mol/L/min. Subsequent computational analysis elucidated the three-dimensional architecture of the enzyme and identified the binding site for the substrate trehalose-6-phosphate (T6P). T6P was found to form hydrogen bonds with TPP at residues Lys754, Arg720, His665, Glu758, and Asn756. Additionally, hydrophobic interactions were observed between T6P and residues Phe802, Ile610, Asp801, Pro752, and Gly753. The binding energy calculated for the T6P-TPP complex stood at -5.7 kcal/mol.
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