Zoologisches Institut - Strukturbiologie, Christian-Albrechts-Universität Kiel, Kiel, Germany; Pharmazeutisches Institut, Christian-Albrechts-Universität Kiel, Kiel, Germany.
Zoologisches Institut - Strukturbiologie, Christian-Albrechts-Universität Kiel, Kiel, Germany.
J Biol Chem. 2023 Nov;299(11):105306. doi: 10.1016/j.jbc.2023.105306. Epub 2023 Sep 29.
The mitochondrial amidoxime-reducing component (mARC) is one of five known molybdenum enzymes in eukaryotes. mARC belongs to the MOSC domain superfamily, a large group of so far poorly studied molybdoenzymes. mARC was initially discovered as the enzyme activating N-hydroxylated prodrugs of basic amidines but has since been shown to also reduce a variety of other N-oxygenated compounds, for example, toxic nucleobase analogs. Under certain circumstances, mARC might also be involved in reductive nitric oxide synthesis through reduction of nitrite. Recently, mARC enzymes have received a lot of attention due to their apparent involvement in lipid metabolism and, in particular, because many genome-wide association studies have shown a common variant of human mARC1 to have a protective effect against liver disease. The mechanism linking mARC enzymes with lipid metabolism remains unknown. Here, we give a comprehensive overview of what is currently known about mARC enzymes, their substrates, structure, and apparent involvement in human disease.
线粒体酰胺还原酶(mARC)是真核生物中已知的五种钼酶之一。mARC 属于 MOSC 结构域超家族,这是一个迄今为止研究甚少的大型钼酶家族。mARC 最初被发现是激活 N-羟化基本脒前药的酶,但此后已被证明还能还原多种其他 N-氧化化合物,例如有毒的核苷类似物。在某些情况下,mARC 还可能通过还原亚硝酸盐参与还原型一氧化氮的合成。最近,mARC 酶由于其明显参与脂质代谢而受到广泛关注,特别是因为许多全基因组关联研究表明,人类 mARC1 的一种常见变体对肝脏疾病具有保护作用。将 mARC 酶与脂质代谢联系起来的机制尚不清楚。本文综述了目前已知的 mARC 酶及其底物、结构和在人类疾病中的明显作用。