A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.
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|
|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; |
entries corresponding to 1.17.4.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.17.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-