UniProt ID: Q58EJ9 |
FUNCTION: Catalyzes the reduction of N-oxygenated molecules, acting as a counterpart of cytochrome P450 and flavin-containing monooxygenases in metabolic cycles. As a component of prodrug-converting system, reduces a multitude of N-hydroxylated prodrugs particularly amidoximes, leading to increased drug bioavailability. May be involved in mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating endogenous nitric oxide levels and biosynthesis. 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. {ECO:0000250|UniProtKB:Q5VT66}. CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N(omega)-hydroxy-L- arginine = 2 Fe(III)-[cytochrome b5] + H2O + L-arginine; Xref=Rhea:RHEA:61644, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:32682, ChEBI:CHEBI:60107; Evidence={ECO:0000250|UniProtKB:Q5VT66}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61645; Evidence={ECO:0000250|UniProtKB:Q5VT66}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250|UniProtKB:Q5VT66}; Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. {ECO:0000250|UniProtKB:Q5VT66}; SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q5VT66}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q5VT66}. Membrane {ECO:0000250|UniProtKB:Q5VT66}; Lipid-anchor {ECO:0000250|UniProtKB:Q5VT66}. Note=Mitochondrial import is mediated by AA 1-36 and requires ATP. {ECO:0000250|UniProtKB:Q5VT66}. DOMAIN: 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. {ECO:0000250|UniProtKB:Q5VT66}. |
UniProt ID: F1QNZ1 |
CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + N(omega)-hydroxy-L- arginine = 2 Fe(III)-[cytochrome b5] + H2O + L-arginine; Xref=Rhea:RHEA:61644, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:32682, ChEBI:CHEBI:60107; Evidence={ECO:0000256|ARBA:ARBA00029322}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61645; Evidence={ECO:0000256|ARBA:ARBA00029322}; |
This information was provided by UniProt through a collaboration with ZFIN. (1) |