Bucciarelli Tonino, Sacchetta Paolo, Amicarelli Fernanda, Petruzzelli Raffaele, Melino Sonia, Rotilio Domenico, Celli Nicola, Di Ilio Carmine
Dipartimento di Scienze Biomediche, Università G. D'Annunzio, Chieti, Italy.
Int J Biochem Cell Biol. 2002 Oct;34(10):1286-90. doi: 10.1016/s1357-2725(02)00066-3.
To investigate structural relationship between amphibian and mammalian GSTs the complete amino acid sequence of the major form of glutathione transferase present in toad liver (Bufo bufo) was determined. The enzyme subunit is composed of 210 amino acid residues corresponding to a molecular mass of 24,178 Da. In comparison with the primary structure of amphibian bbGSTP1-1, toad liver GST showed 54% sequence identity. On the other hand, toad liver GST showed about 45-55% sequence identity when compared with other pi class GST and less then 25% identity with GST of other classes. Amino acid residues involved in the H site and in the key and lock structure of the toad enzyme are significantly different from those of bbGSTP1-1 and other mammalian pi class GST. On the basis of its structural and immunological properties the toad liver GST, indicated as bbGSTP2-2, could represent the prototype of a subset of the pi family.
为了研究两栖动物和哺乳动物谷胱甘肽S-转移酶(GSTs)之间的结构关系,测定了蟾蜍肝脏(Bufo bufo)中主要形式的谷胱甘肽转移酶的完整氨基酸序列。该酶亚基由210个氨基酸残基组成,分子量为24,178 Da。与两栖动物bbGSTP1-1的一级结构相比,蟾蜍肝脏GST显示出54%的序列同一性。另一方面,与其他pi类GST相比,蟾蜍肝脏GST显示出约45-55%的序列同一性,与其他类别的GST同一性低于25%。蟾蜍酶的H位点以及钥匙和锁结构中涉及的氨基酸残基与bbGSTP1-1和其他哺乳动物pi类GST的氨基酸残基有显著差异。基于其结构和免疫特性,蟾蜍肝脏GST被命名为bbGSTP2-2,它可能代表pi家族一个亚组的原型。