摘要
为了了解条斑紫菜海藻酸盐裂解酶PyAly(Porphyra yezoensis alginate lyase)的结构与功能,试验通过生物信息学方法分析其理化性质、信号肽、跨膜区、亚细胞定位、结构及进行多序列比对,并将建模得到的结构进行分子动力学模拟。结果表明:PyAly为亲水性蛋白,N端1-25位为信号肽,下游区域位于胞内,二级结构中无规则卷曲和α-螺旋占比较高,三级结构具有明显β-jellyroll结构,属于PL-7蛋白家族,尚未发现与其同源性较高的真核生物来源蛋白,活性位点处的保守氨基酸残基对其功能的发挥具有重要作用。优化后的蛋白结构较为合理,可为PyAly酶解机理研究奠定基础。
To understand the structure and function of PyAly(Porphyra yezoensis alginate lyase), physicochemical properties, signal peptide, transmembrane helices, subcellular localization, structure and multi-sequence alignment were predicted and analyzed by bioinformatics. The top quality model was selected and optimized with molecular dynamic simulation. Results show that PyAly is a hydrophilic protein. The 25 amino acids located at the N-terminus are predicted to be a signal peptide, and the protein is located inside the cell. Radom coils and α-helices account for a high proportion in secondary structure. PyAly belongs to PL-7 family with β-jellyroll structure. No high identity protein has been identified thus far with eukaryotes. Conserved amino acid residues surrounding the active site play an important role in catalysis. The predicted structure will lay a solid foundation for studying the mechanism of enzymolysis.
作者
吴承燕
苏羽航
Wu Chengyan;Su Yuhang(Fujian Universities and Colleges Engineering Research Center of Soft Plastic Packaging Technology for Food,Fujian Provincial Key Lab of Coastal Basin Environment,Fuqing Branch of Fujian Normal University,Fuqing 350300,China)
出处
《广东化工》
CAS
2020年第13期11-13,共3页
Guangdong Chemical Industry
基金
福建省教育厅A类项目(JA15578)
食品软塑包装技术福建省高校工程研究中心开放基金项目(G1-KF1704)。