期刊
FEMS MICROBIOLOGY LETTERS
卷 289, 期 1, 页码 41-45出版社
OXFORD UNIV PRESS
DOI: 10.1111/j.1574-6968.2008.01372.x
关键词
peroxiredoxin; thioredoxin; thiol peroxidase; periplasm; osmotic shock
类别
资金
- NIG, Japan
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.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据