The former consists of glutathione, glutathione reductase and glutaredoxin, while the later consists of thioredoxin and thioredoxin reductase.
谷氧还蛋白属于硫氧还蛋白超家族，广泛分布在各种生物体内。
Thioredoxin reductase
英语例句库
中文百科
硫氧还蛋白还原酶
硫氧还蛋白还原酶（英语：thioredoxin reductase），缩写为TrxR或者TR，是一种NADPH依赖的包含FAD结构域的还原酶，活性形式通常为二聚体，属于吡啶核苷酸-二硫化物氧化还原酶家族。顾名思义，硫氧还蛋白还原酶是用来还原它的生理底物硫氧化蛋白的酶。它和硫氧还蛋白（Trx）、NADPH共同构成了硫氧还蛋白系统（Trx system）。哺乳动物体系的硫氧还蛋白还原酶属于硒蛋白。硫氧还蛋白还原酶有很多生物学功能，与人类某些疾病发病机制密切相关，目前在癌症研究中亦作为重要的抗癌靶点，受到广泛关注和深入研究。
英语百科
Thioredoxin reductase 硫氧还蛋白还原酶
![Schematic diagram of TrxR's cellular role Adapted from Holmgren et al.[3]](/uploads/202502/16/CellularTrxR0101.png)
![Proposed mechanism in mammals and presumably humans: Starting from the completely oxidized form, the reaction begins with the reduction of the selenenylsulfide to the selenolate anion (Se(-1)) with electrons received from NADPH via FAD (Step A). Due to the low pKa value of the selenol the selenolate anion is the predominant form under physiological conditions. A second electron transfer from a second molecule of NADPH reduces the active site tihiol bonds with one Cys residue stabilized by an interaction with FAD (Step B). The selenolate anion then attacks the disulfide bonds of Trx and the resulting enzyme-Trx mixed selenenylsulfide (Step C), which is then subsequently attacked by the neighboring Cys residue to regenerate the selenenylsulfide (Step D). This selenenylsulfide is then reduced by the active-site thiolate from the other subunit (Step E). Adapted from Zhong et al.[11] Consistent with findings that (2,2‘:6‘,2‘‘-terpyridine)platinum(II) complexes inhibit human TrxR.[12]](/uploads/202502/16/HumanTrxRRxnMech0101.jpg)
Thioredoxin reductases (TR, TrxR) (EC1.8.1.9) are the only known enzymes to reduce thioredoxin (Trx). Two classes of thioredoxin reductase have been identified: one class in bacteria and some eukaryotes and one in animals. Both classes are flavoproteins which function as homodimers. Each monomer contains a FAD prosthetic group, a NADPH binding domain, and an active site containing a redox-active disulfide bond.
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