ENZYME entry: EC 126.96.36.199
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|Ribonucleoside-triphosphate reductase (formate).
|Anaerobic ribonucleoside-triphosphate reductase.|
|Ribonucleoside 5'-triphosphate + formate <=> 2'-deoxyribonucleoside 5'-triphosphate + CO(2) + H(2)O|
- 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
- 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 (1-lambda(4)-disulfan-1-yl) radical
bridge between methionine and cysteine residues.
- Oxidation of formate by the thiosulfuranyl radical results in the
release of CO(2) and regeneration of the thiyl radical.
- Cf. EC 188.8.131.52 and EC 184.108.40.206.
|PRIAM enzyme-specific profiles||220.127.116.11|
|KEGG Ligand Database for Enzyme Nomenclature||18.104.22.168|
|IUBMB Enzyme Nomenclature||22.214.171.124|
|MEDLINE||Find literature relating to 126.96.36.199|
|Rhea expert-curated reactions||188.8.131.52|
entries corresponding to 1.1.98.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-