【摘要】 γ-谷氨酰转肽酶(γ-GGT)是催化L-茶氨酸合成的关键酶之一,对其编码基因的解析有助于进行茶氨酸的合成调控和异源表达生产研究,本论文利用生物信息学方法,对大肠杆菌(Escherichia coli)γ-GGT基因的结构和特性进行分析。结果显示,E.coliγ-GGT基因编码580个氨基酸,主要氨基酸为甘氨酸和亮氨酸,γ-GGT酶蛋白等电点为5.38,分子量为61.7 kDa,属于酸性不稳定亲水性蛋白,具有信号肽序列和保守功能结构域,在细胞质周质中发挥作用,其二级结构元件主要是α-螺旋和无规卷曲,在微生物中进化较为保守。研究结果为进一步研究γ-GGT基因功能及其应用奠定了基础。更多还原

【Abstract】 γ-Glutamyltranspeptidase(γ-GGT) is one of the key enzymes catalyzing the synthesis of L-theanine. Analyzing its coding gene is great significance for the production of theanine. In this study, a bioinformatics approach was used to analyse the structure and function of genes in Escherichia coli γ-GGT. The results showed that the γ-GGT gene of E.coli encoded 580 amino acids. The main amino acids were Gly and Leu. The isoelectric point of γ-GGT enzyme protein was 5.38 with a molecular weight of 61.7 kDa. It was an unstable hydrophilic protein and had a signal peptide sequence and a conserved functional domain and played a role in the periplasm. The secondary structural elements were mainly Helix and Coil, which played a conservative role in the evolution.更多还原