ENZYME entry: EC 184.108.40.206
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|Ribonucleoside-triphosphate reductase (thioredoxin).
|2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H(2)O <=> ribonucleoside triphosphate + thioredoxin|
- The enzyme, characterized from the bacterium Lactobacillus
leichmannii, is similar to class II ribonucleoside-diphosphate
reductase (cf. EC 220.127.116.11); 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
- This radical attacks the substrate, forming a ribonucleotide
3'-radical, followed by water loss to form a ketyl (alpha-oxoacyl)
- The ketyl radical is reduced to 3'-keto-deoxynucleotide concomitant
with formation of a disulfide anion radical between two cysteine
- A proton-coupled electron-transfer from the disulfide radical to the
substrate generates a 3'-deoxynucleotide radical, and the 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 18.104.22.168.
|PRIAM enzyme-specific profiles||22.214.171.124|
|KEGG Ligand Database for Enzyme Nomenclature||126.96.36.199|
|IUBMB Enzyme Nomenclature||188.8.131.52|
|MEDLINE||Find literature relating to 184.108.40.206|
|P07071, NRDD_BPT4; ||P28903, NRDD_ECOLI; ||P43752, NRDD_HAEIN; |
|Q9L646, NRDD_SALTY; ||Q54CW7, RTPR_DICDI; ||Q2PDF6, RTPR_EUGGR; |
|Q5FMX8, RTPR_LACAC; ||Q03PB4, RTPR_LACBA; ||Q1G7W2, RTPR_LACDA; |
|Q04CQ7, RTPR_LACDB; ||Q041L3, RTPR_LACGA; ||A8YW74, RTPR_LACH4; |
|Q59490, RTPR_LACLE; ||Q035U1, RTPR_LACP3; ||A6Q367, RTPR_NITSB; |
|Q857H2, VG50_BPMB2; ||O64240, VG50_BPMD2; ||Q05262, VG50_BPML5; |
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