Bhargavi Rayavarapu, Vishwakarma Siddharth, Murty Upadhyayula Suryanarayana
Bioinformatics Group, Biology Division, Indian Institute of Chemical Technology, Hyderabad, India.
Bioinformation. 2005 Jun 2;1(1):25-7. doi: 10.6026/97320630001025.
GST (glutathione S-transferases) are a family of detoxification enzymes that catalyze the conjugation of reduced GSH (glutathione) to xenobiotic (endogenous electrophilic) compounds. GST from Wb (Wuchereria bancrofti) and Bm (Brugia malayi) are significantly different from human GST in sequence and structure. Thus, Wb-GST and Bm-GST are potential chemotherapeutic targets for anti-filarial treatment. Comparison of modeled Wb and Bm GST with human GST show structural difference between them. Analysis of the active site residues for the binding of electrophilic co-substrates provides insight towards the design of parasite specific GST inhibitors.
谷胱甘肽S-转移酶(GST)是一类解毒酶,可催化还原型谷胱甘肽(GSH)与外源性(内源性亲电)化合物的结合。来自班氏吴策线虫(Wuchereria bancrofti)和马来布鲁线虫(Brugia malayi)的GST在序列和结构上与人类GST有显著差异。因此,班氏吴策线虫GST和马来布鲁线虫GST是抗丝虫治疗的潜在化疗靶点。将模拟的班氏吴策线虫和马来布鲁线虫GST与人类GST进行比较,显示出它们之间的结构差异。分析亲电共底物结合的活性位点残基,有助于设计针对寄生虫的GST抑制剂。