MARC1,MARC2 reduce N-hydroxylated compounds

Stable Identifier
R-HSA-8936442
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Mitochondrial amidoxime-reducing components 1 and 2 (MARC1 and 2) are Mo-molybdopterin (Mo-MPT) cofactor-dependent, outer mitochondrial membrane-associated enzymes capable of reducing N-hydroxylated prodrugs and N-hydroxy-L-arginine (NOHA) and N-hydroxy-N-methyl-L-arginine (NHAM) into L-arginine and N(delta)-methyl-L-arginine, respectively. They are components of an N-hydroxylated prodrug-converting complex, also containing cytochrome b5 (CYB5B) and NADH cytochrome b5 reductase 3 (CYB5R3) (Jakobs et al. 2014, Gruenewald et al. 2008, Ott et al. 2014, 2015). The reduction of NOHA is described in this reaction.

Literature References
PubMed ID Title Journal Year
25144769 The N-reductive system composed of mitochondrial amidoxime reducing component (mARC), cytochrome b5 (CYB5B) and cytochrome b5 reductase (CYB5R) is regulated by fasting and high fat diet in mice

Jakobs, HH, Mikula, M, Havemeyer, A, Strzalkowska, A, Borowa-Chmielak, M, Dzwonek, A, Gajewska, M, Hennig, EE, Ostrowski, J, Clement, B

PLoS ONE 2014
25425164 The mammalian molybdenum enzymes of mARC

Ott, G, Havemeyer, A, Clement, B

J. Biol. Inorg. Chem. 2015
19053771 The fourth molybdenum containing enzyme mARC: cloning and involvement in the activation of N-hydroxylated prodrugs

Gruenewald, S, Wahl, B, Bittner, F, Hungeling, H, Kanzow, S, Kotthaus, J, Schwering, U, Mendel, RR, Clement, B

J. Med. Chem. 2008
24423752 Functional characterization of protein variants encoded by nonsynonymous single nucleotide polymorphisms in MARC1 and MARC2 in healthy Caucasians

Ott, G, Reichmann, D, Boerger, C, Cascorbi, I, Bittner, F, Mendel, RR, Kunze, T, Clement, B, Havemeyer, A

Drug Metab. Dispos. 2014
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
oxidoreductase activity of MARC1:Mo-MPT:MARC2:Mo-MPT:CYB5B:CYB5R3 [mitochondrial outer membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created