Mitochondrial amidoxime-reducing component 1

Comprises two structural domains, the molybdenum cofactor/Moco sulfurase C-terminal (MOSC) domain and the MOSC N-terminal region, forming a cleft that accommodates Moco. The MOSC domain, which contains a large seven-stranded mostly antiparallel beta-barrel, engages multiple interactions with Moco both pterin ring and phosphate group, allowing for a tight coordination of Moco within the core of the enzyme.

Catalyzes the reduction of N-oxygenated molecules, acting as a counterpart of cytochrome P450 and flavin-containing monooxygenases in metabolic cycles (PubMed:19053771, PubMed:21029045, PubMed:30397129). As a component of prodrug-converting system, reduces a multitude of N-hydroxylated prodrugs particularly amidoximes, leading to increased drug bioavailability (PubMed:19053771). May be involved in mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating endogenous nitric oxide levels and biosynthesis (PubMed:21029045). Postulated to cleave the N-OH bond of N-hydroxylated substrates in concert with electron transfer from NADH to cytochrome b5 reductase then to cytochrome b5, the ultimate electron donor that primes the active site for substrate reduction (PubMed:19053771, PubMed:21029045).

• Mitochondrion outer membrane
• Single-pass type II membrane protein
• Membrane
• Lipid-anchor
• Mitochondrial import is mediated by AA 1-40 and requires ATP.

MARC1, MOSC1, MTARC1, Mitochondrial amidoxime-reducing component 1, mARC1, Molybdenum cofactor sulfurase C-terminal domain-containing protein 1, MOSC domain-containing protein 1, Moco sulfurase C-terminal domain-containing protein 1

• entrezGene:64757
• swissprot:Q5VT66

Proteins

Metabolism

37499Da