Zimniak P, Eckles M A, Saxena M, Awasthi Y C
Department of Medicine, University of Arkansas for Medical Sciences, Little Rock 72205.
FEBS Lett. 1992 Nov 23;313(2):173-6. doi: 10.1016/0014-5793(92)81438-r.
A full-length cDNA clone encoding the previously purified mouse glutathione S-transferase GST 5.7 [(1991), Biochem. J. 278, 793-799] has been isolated from a mouse lung cDNA library in lambda gt11. Sequencing of the clone revealed the presence of microheterogeneity in GST 5.7. Comparison of the deduced protein sequence with other glutathione S-transferases, together with previous information available on GST 5.7, indicates that the enzyme belongs to a novel subgroup within the alpha class of glutathione S-transferases. Members of the subgroup, which also include the rat GST 8-8 and perhaps chicken GST CL3, show high sequence homology with each other, but only moderate similarity to other alpha class enzymes. They share a substrate specificity profile that resembles pi-class enzymes, and are active in the conjugation of lipid peroxidation products.
已从λgt11载体中的小鼠肺cDNA文库中分离出一个全长cDNA克隆,该克隆编码先前纯化的小鼠谷胱甘肽S-转移酶GST 5.7([1991年,《生物化学杂志》278卷,793 - 799页])。对该克隆进行测序后发现GST 5.7存在微异质性。将推导得到的蛋白质序列与其他谷胱甘肽S-转移酶进行比较,结合之前关于GST 5.7的信息表明,该酶属于谷胱甘肽S-转移酶α类中的一个新亚组。该亚组的成员还包括大鼠GST 8 - 8以及可能的鸡GST CL3,它们彼此之间具有高度的序列同源性,但与其他α类酶仅有中等程度的相似性。它们具有类似于π类酶的底物特异性谱,并且在脂质过氧化产物的结合反应中具有活性。