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比较基因组学分析分枝杆菌 NrdH-氧化还原酶。

Comparative genomics analysis of Mycobacterium NrdH-redoxins.

机构信息

Institute of Modern Biopharmaceuticals, School of Life Sciences, Southwest University, Chongqing 400715, China.

出版信息

Microb Pathog. 2010 Mar-Apr;48(3-4):97-102. doi: 10.1016/j.micpath.2010.01.004. Epub 2010 Jan 22.

DOI:10.1016/j.micpath.2010.01.004
PMID:20096772
Abstract

NrdH is one of the intracellular redoxins exist in Mycobacterium and other microorganisms lacking the common glutathione system. NrdH seems a chimeric protein of glutaredoxin amino acid sequence and thioredoxin activity. It serves as a hydrogen donor for ribonucleotide reductase. Mycobacterium tuberculosis might take advantage of this enzyme to persist in the highly oxidized host mononuclear phagocytes and maintain the balance of intracellular redox potential. Physiological role of NrdH and comparison of its genomic context organization were summarized here. The most intriguing feature might be its new drug targets potential.

摘要

NrdH 是一种存在于分枝杆菌和其他缺乏常见谷胱甘肽系统的微生物中的细胞内氧化还原酶。NrdH 似乎是谷胱甘肽还原酶氨基酸序列和硫氧还蛋白活性的嵌合蛋白。它是核糖核苷酸还原酶的氢供体。结核分枝杆菌可能利用这种酶在高度氧化的宿主单核吞噬细胞中存活下来,并维持细胞内氧化还原电势的平衡。本文总结了 NrdH 的生理作用及其基因组环境组织的比较。最有趣的特点可能是其作为新药靶点的潜力。

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引用本文的文献

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A shift in the virulence potential of Corynebacterium pseudotuberculosis biovar ovis after passage in a murine host demonstrated through comparative proteomics.通过比较蛋白质组学证明,绵羊伪结核棒状杆菌生物变种在小鼠宿主体内传代后毒力潜力发生了变化。
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NrdH Redoxin enhances resistance to multiple oxidative stresses by acting as a peroxidase cofactor in Corynebacterium glutamicum.
NrdH氧化还原蛋白通过作为谷氨酸棒杆菌中的过氧化物酶辅因子增强对多种氧化应激的抗性。
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