1.1.98.6: ribonucleoside-triphosphate reductase (formate)

This is an abbreviated version!
For detailed information about ribonucleoside-triphosphate reductase (formate), go to the full flat file.

Word Map on EC 1.1.98.6

Reaction

ribonucleoside 5'-triphosphate
+
formate
=
2'-deoxyribonucleoside 5'-triphosphate
+
CO2
+
H2O

Synonyms

anaerobic ribonucleoside-triphosphate reductase, anaerobic ribonucleotide reductase, class III ribonucleoside-triphosphate reductase, nrdD

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.98 With other, known, physiological acceptors
                1.1.98.6 ribonucleoside-triphosphate reductase (formate)

Systematic Name

Systematic Name on EC 1.1.98.6 - ribonucleoside-triphosphate reductase (formate)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
SYSTEMATIC NAME
IUBMB Comments
ribonucleoside-5'-triphosphate:formate 2'-oxidoreductase
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 (1lambda4-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 1.17.4.1, ribonucleoside-diphosphate reductase and EC 1.17.4.2, ribonucleoside-triphosphate reductase (thioredoxin).