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
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1.17.4.2
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hydroxyurea
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deoxyribonucleotides
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dntp
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rr
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herpes
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tyrosyl
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simplex
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gemcitabine
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leukemia
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reductases
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thymidine
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thioredoxins
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deoxycytidine
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deoxynucleotides
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cdp
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s-phase
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thymidylate
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thiosemicarbazone
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glutaredoxins
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checkpoint
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nsclc
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cytidine
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diferric
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deoxyadenosine
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diiron
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fork
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deoxyguanosine
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5'-diphosphate
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nonidentical
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gallium
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antiferromagnetically
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hyperfine
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proton-coupled
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dinuclear
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oncolytic
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cross-complementation
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acyclovir
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cladribine
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chk1
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thiyl
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aphidicolin
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cross-complementing
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endor
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fludarabine
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b12-dependent
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gemcitabine-based
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deoxythymidine
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analysis
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gemcitabine-induced
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high-valent
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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
1.17.4.2 ribonucleoside-triphosphate reductase (thioredoxin)Advanced search results
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results (General Stability
General Stability on EC 1.17.4.2 - ribonucleoside-triphosphate reductase (thioredoxin)
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GENERAL STABILITY 
ORGANISM
UNIPROT
LITERATURE
fairly stable under conditions of storage, losing only about 23% of its activity in 15 months
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immobilization stabilizes the enzyme substantially, compared with free enzyme, which has an inactivation half-life of less than 1 day, on immobilization the inactivation half-life is about 15 days
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