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ENZYME entry: EC

Accepted Name
ribonucleoside-triphosphate reductase (formate).
Alternative Name(s)
anaerobic ribonucleoside-triphosphate reductase.
Reaction catalysed
a ribonucleoside 5'-triphosphate + formate + H(+) <=> a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O
  • The enzyme, which is expressed in the bacterium Escherichia coli during anaerobic growth, contains an iron sulfur center.
  • The active form of the enzyme contains an oxygen-sensitive glycyl (1-amino-2-oxoethan-1-yl) radical that is generated by the activating enzyme NrdG via chemistry involving S-adenosylmethionine (SAM) and a [4Fe-4S] cluster.
  • The glycyl radical is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical.
  • The ketyl radical gains an electron from a cysteine residue and a proton from formic acid, forming 3'-keto-deoxyribonucleotide and generating a thiosulfuranyl (1lambda(4)-disulfan-1-yl) radical bridge between methionine and cysteine residues.
  • Oxidation of formate by the thiosulfuranyl radical results in the release of CO2 and regeneration of the thiyl radical.
  • Cf. EC and EC
PRIAM enzyme-specific profiles1.1.98.6
KEGG Ligand Database for Enzyme Nomenclature1.1.98.6
IUBMB Enzyme Nomenclature1.1.98.6
MEDLINEFind literature relating to
Rhea expert-curated reactions1.1.98.6
P07071, NRDD_BPT4;  P28903, NRDD_ECOLI;  P43752, NRDD_HAEIN;  

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