期刊
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
卷 20, 期 2, 页码 265-275出版社
SPRINGER
DOI: 10.1007/s00775-014-1216-4
关键词
mARC; Moco; MOSC; Biotransformation; Amidoxime
资金
- Deutsche Forschungsgemeinschaft [DFG] [Cl 56/9-1, ME 1266/24-1]
The mitochondrial amidoxime reducing component (mARC) is the most recently discovered molybdenum-containing enzyme in mammals. All mammalian genomes studied to date contain two mARC genes: MARC1 and MARC2. The proteins encoded by these genes are mARC-1 and mARC-2 and represent the simplest form of eukaryotic molybdenum enzymes, only binding the molybdenum cofactor. In the presence of NADH, mARC proteins exert N-reductive activity together with the two electron transport proteins cytochrome b(5) type B and NADH cytochrome b(5) reductase. This enzyme system is capable of reducing a great variety of N-hydroxylated substrates. It plays a decisive role in the activation of prodrugs containing an amidoxime structure, and in detoxification pathways, e.g., of N-hydroxylated purine and pyrimidine bases. It belongs to a group of drug metabolism enzymes, in particular as a counterpart of P450 formed N-oxygenated metabolites. Its physiological relevance, on the other hand, is largely unknown. The aim of this article is to summarize our current knowledge of these proteins with a special focus on the mammalian enzymes and their N-reductive activity.
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