Identification, characterization, and crystal structure of the omega class glutathione transferases
Identification, characterization, and crystal structure of the omega class glutathione transferases
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DOI：
10.1074/jbc.m001706200
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发表时间：
2000-08-11
影响因子：
4.8
通讯作者：
Pandit, J
中科院分区：
文献类型：
--
作者：
Board, PG;Coggan, M;Pandit, J
通过对表达序列标签数据库的分析和序列比对发现了一类新的谷胱甘肽转移酶，这类新的谷胱甘肽S-转移酶（GST），命名为Omega，存在于几种哺乳动物物种和秀丽隐杆线虫中。在人类中，GSTO 1-1在大多数组织中表达，并表现出谷胱甘肽依赖性巯基转移酶和脱氢抗坏血酸还原酶活性，GSTO 1-1的结构已在2.0埃分辨率下确定，并具有特征性GST折叠（蛋白质数据库条目代码leem）。欧米茄类GST表现出不寻常的N-末端延伸，邻接C末端形成一个新的结构单元。与其他哺乳动物GST不同，GSTO 1-1似乎具有可与谷胱甘肽形成二硫键的活性位点半胱氨酸，
A new class of glutathione transferases has been discovered by analysis of the expressed sequence tag data base and sequence alignment, Glutathione S-transferases (GSTs) of the new class, named Omega, exist in several mammalian species and Caenorhabditis elegans, In humans, GSTO 1-1 is expressed in most tissues and exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities characteristic of the glutaredoxins, The structure of GSTO 1-1 has been determined at 2.0-Angstrom resolution and has a characteristic GST fold (Protein Data Bank entry code leem). The Omega class GSTs exhibit an unusual N-terminal extension that abuts the C terminus to form a novel structural unit. Unlike other mammalian GSTs, GSTO 1-1 appears to have an active site cysteine that can form a disulfide bond with glutathione,