RNR (M1M2B) reduces nucleotide diphosphates to deoxynucleotide diphosphates (glutaredoxin)
NDP(3-) + GLRX → dNDP(3-) + 2xHC-GLRX + H2O
- Reactome
- R-HSA-8866405
- Compartment
- cytosol
- Rhea
- None recorded
Inputs
- NDP(3-)CHEBI:57930, C5H8O10P2R, cytosol
- GLRXR-HSA-55729, cytosol
Outputs
- dNDP(3-)CHEBI:73316, C5H8O9P2R, cytosol
- 2xHC-GLRXR-HSA-111740, cytosol
- H2OCHEBI:15377, H2O, cytosol
Catalysed by
- ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor of RNR (M1M2B) [cytosol]
Literature
- Structure and function of the radical enzyme ribonucleotide reductase Prog Biophys Mol Biol, 2001
- Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells J Biol Chem, 2001
- Thioredoxin and glutaredoxin systems J Biol Chem, 1989
- Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage Proc. Natl. Acad. Sci. U.S.A., 2008
- Mammalian ribonucleotide reductase subunit p53R2 is required for mitochondrial DNA replication and DNA repair in quiescent cells Proc. Natl. Acad. Sci. U.S.A., 2012
- Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase J Biol Chem, 2000