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
-
1.17.4.2
-
hydroxyurea
-
deoxyribonucleotides
-
dntp
-
rr
-
herpes
-
tyrosyl
-
simplex
-
gemcitabine
-
leukemia
-
reductases
-
thymidine
-
thioredoxins
-
deoxycytidine
-
deoxynucleotides
-
cdp
-
s-phase
-
thymidylate
-
thiosemicarbazone
-
glutaredoxins
-
checkpoint
-
nsclc
-
cytidine
-
diferric
-
deoxyadenosine
-
diiron
-
fork
-
deoxyguanosine
-
5'-diphosphate
-
nonidentical
-
gallium
-
antiferromagnetically
-
hyperfine
-
proton-coupled
-
dinuclear
-
oncolytic
-
cross-complementation
-
acyclovir
-
cladribine
-
chk1
-
thiyl
-
aphidicolin
-
cross-complementing
-
endor
-
fludarabine
-
b12-dependent
-
gemcitabine-based
-
deoxythymidine
-
analysis
-
gemcitabine-induced
-
high-valent
-
peroxo
- 1.17.4.2
- hydroxyurea
- deoxyribonucleotides
- dntp
- rr
- herpes
-
tyrosyl
- simplex
- gemcitabine
- leukemia
- reductases
- thymidine
- thioredoxins
- deoxycytidine
-
deoxynucleotides
- cdp
-
s-phase
- thymidylate
- thiosemicarbazone
- glutaredoxins
-
checkpoint
-
nsclc
- cytidine
-
diferric
- deoxyadenosine
-
diiron
-
fork
- deoxyguanosine
- 5'-diphosphate
-
nonidentical
- gallium
-
antiferromagnetically
-
hyperfine
-
proton-coupled
-
dinuclear
-
oncolytic
-
cross-complementation
- acyclovir
- cladribine
- chk1
-
thiyl
- aphidicolin
-
cross-complementing
-
endor
- fludarabine
-
b12-dependent
-
gemcitabine-based
- deoxythymidine
- analysis
-
gemcitabine-induced
-
high-valent
-
peroxo
Reaction
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
Advanced search results
General Information
General Information 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.
metabolism
-
RNR is the rate-limiting enzyme in deoxyribonucleoside triphosphate, dNTP, biosynthesis
physiological function
additional information
-
during anaerobic growth, Escherichia coli depends on a class III RNR for the synthesis of deoxyribonucleotides
physiological function
-
RNR is the rate-limiting enzyme in deoxyribonucleoside triphosphate, dNTP, biosynthesis, with important roles in nuclear genome maintenance. RNR is also essential for maintenance of mitochondrial DNA in mammals
physiological function
-
role of RNRs during infection of macrophages and epithelial cells, overview. Class II RNR is not responsible for deoxyribonucleotide production during invasion and proliferation inside macrophages and epithelial cells
physiological function
-
the enzyme is involved in ribonucleotide reduction, that provides deoxynucleotides for nuclear and mitochondrial DNA replication and DNA repair
-
cycling fibroblasts from a patient with a lethal mutation in p53R2 contain a normal amount of mtDNA and show normal growth, ribonucleotide reduction, and deoxynucleoside triphosphate (dNTP) pools. However, when made quiescent by prolonged serum starvation the mutant cells strongly down-regulate ribonucleotide reduction, decrease their dCTP and dGTP pools, and virtually abolish the catabolism of dCTP in substrate cycles. mtDNA is not affected
additional information
Tequatrovirus T4
-
Cys290 in class III from bacteriophage T4 are the conserved cysteine residues that are the sites for generation of the thiyl radical
additional information
-
high-level overexpression of RNR subunits, Rrm1, Rrm2 and p53R2, separately or in different combinations, in mice does not result in mtDNA copy number elevation. Instead, simultaneous expression of two RNR subunits leads to imbalanced dNTP pools and progressive mtDNA depletion in the skeletal muscle, without mtDNA mutagenesis, overview
additional information
-
RNRs are allosterically regulated on two levels, overall activity and substrate specificity. The substrate specificity is regulated by the binding of dNTPs to the specificity site, ATP and dATP upregulate the reduction of CDP and UDP, whereas dTTP upregulates GDP reduction and dGTP increases the rate of ADP reduction. This regulation is essential to maintain balanced dNTP pools for DNA synthesis and repairI
additional information
-
RNRs are allosterically regulated on two levels, overall activity and substrate specificity. The substrate specificity is regulated by the binding of dNTPs to the specificity site, ATP and dATP upregulate the reduction of CDP and UDP, whereas dTTP upregulates GDP reduction and dGTP increases the rate of ADP reduction. This regulation is essential to maintain balanced dNTP pools for DNA synthesis and repairI
additional information
-
RNRs are allosterically regulated on two levels, overall activity and substrate specificity. The substrate specificity is regulated by the binding of dNTPs to the specificity site, ATP and dATP upregulate the reduction of CDP and UDP, whereas dTTP upregulates GDP reduction and dGTP increases the rate of ADP reduction. This regulation is essential to maintain balanced dNTP pools for DNA synthesis and repairI
additional information
-
the class II RNR reaction involves deoxyadenosyl or cysteinyl radicals and is independent of oxygen. The thiyl radical in class II RNR is believed to be generated directly at the active site using the cofactor 5'-deoxyadenosylcobalamin
additional information
-
the class II RNR reaction involves deoxyadenosyl or cysteinyl radicals and is independent of oxygen. The thiyl radical in class II RNR is believed to be generated directly at the active site using the cofactor 5'-deoxyadenosylcobalamin
additional information
-
the class III RNR reaction involves deoxyadenosyl, glycyl, or cysteinyl radicals and requires anaerobic conditions
additional information
-
transcriptional regulation of RNR classes as well as their differential function during infection of macrophage and epithelial cells, overview
additional information
-
comparative analyses of ribonucleotide reductase homologs. Results of homology modeling studies indicate that most of the bifidobacteria-specific conserved signature indels are located within the surface loops of the ribonucleotide reductases, and of these, a large 43 amino acid insert in the class III ribonucleotide reductase homolog forms an extension of the allosteric regulatory site known to be essential for protein function. Preliminary docking studies suggest that this large conserved signature indels may be playing a role in enhancing the stability of the RNR dimer complex