Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.17.4.2: ribonucleoside-triphosphate reductase (thioredoxin)

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

Word Map on EC 1.17.4.2

Reaction

2'-deoxyribonucleoside 5'-triphosphate
+
thioredoxin disulfide
+
H2O
=
ribonucleoside 5'-triphosphate
+
thioredoxin

Synonyms

2'-deoxyribonucleoside-triphosphate:oxidized-thioredoxin 2'-oxidoreductase, adenosylcobalamin-dependent ribonucleoside-triphosphate reductase, class Ib ribonucleotide reductase, class Ib RNR, class II ribonucleotide reductase, class II RNR, class III ribonucleotide reductase, class III RNR, More, nrdD, nucleoside triphosphate reductase, ribonucleoside triphosphate reductase, ribonucleotide diphosphate reductase, ribonucleotide reductase, RNR, RNR class Ia, RNR2, RTPR

ECTree

     1 Oxidoreductases
         1.17 Acting on CH or CH2 groups
             1.17.4 With a disulfide as acceptor
                1.17.4.2 ribonucleoside-triphosphate reductase (thioredoxin)

Systematic Name

Systematic Name on EC 1.17.4.2 - ribonucleoside-triphosphate reductase (thioredoxin)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
SYSTEMATIC NAME
IUBMB Comments
2'-deoxyribonucleoside-5'-triphosphate:thioredoxin-disulfide 2'-oxidoreductase
The enzyme, characterized from the bacterium Lactobacillus leichmannii, is similar to class II ribonucleoside-diphosphate reductase (cf. EC 1.17.4.1). However, it is specific for the triphosphate versions of its substrates. The enzyme contains an adenosylcobalamin cofactor that is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue. This radical attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical. The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant with formation of a disulfide anion radical between two cysteine residues. A proton-coupled electron-transfer from the disulfide radical to the substrate generates a 3'-deoxynucleotide radical, and the final product is formed when the hydrogen atom that was initially removed from the 3'-position of the nucleotide by the thiyl radical is returned to the same position. The disulfide bridge is reduced by the action of thioredoxin. cf. EC 1.1.98.6, ribonucleoside-triphosphate reductase (formate).