Subcellular localization and in vivo oxidation-reduction kinetics of thiol peroxidase in Escherichia coli.
Subcellular localization and in vivo oxidation-reduction kinetics of thiol peroxidase in Escherichia coli.
复制标题
大肠杆菌中硫醇过氧化物酶的亚细胞定位和体内氧化还原动力学。
DOI：
10.1111/j.1574-6968.2008.01372.x
复制
发表时间：
2008
影响因子：
2.1
通讯作者：
K. Tao
中科院分区：
文献类型：
--
作者：
K. Tao
Peroxiredoxins are a class of peroxide-scavenging enzymes having a conserved cysteine residue(s) in their active centers. Thiol peroxidase (Tpx) is one of the peroxiredoxins identified in Escherichia coli. Despite the absence of the N-terminal signal sequence for transport across the membrane, it has been characterized as a periplasmic protein. Reanalysis of Tpx localization, using active site cysteine mutants of thioredoxin 1 (Trx1), demonstrated that Tpx forms a mixed-disulfide complex with cytoplasmic Trx1, indicating that Tpx localizes in the cytoplasm.
来自大肠杆菌的硫氧还蛋白在渗透敏感室中的定位。
DOI：
--
发表时间：
1982
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Lunn,CA;Pigiet,VP
通讯作者：
Pigiet,VP