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Information on EC 1.17.4.2 - ribonucleoside-triphosphate reductase (thioredoxin)
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1.17.4.2 ribonucleoside-triphosphate reductase (thioredoxin)IUBMB Comments
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).
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Word Map
- 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
The enzyme appears in viruses and cellular organisms
Synonyms
ribonucleotide reductase, rtpr, class ib rnr, ribonucleoside triphosphate reductase, class ii rnr, class iii rnr, class ib ribonucleotide reductase, ribonucleotide diphosphate reductase, class iii ribonucleotide reductase, class ii ribonucleotide reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2'-deoxyribonucleoside-triphosphate:oxidized-thioredoxin 2'-oxidoreductase
-
-
-
-
adenosylcobalamin-dependent ribonucleoside-triphosphate reductase
-
class II RNR
class III RNR
ribonucleoside triphosphate reductase
ribonucleotide reductase
RNR
RNR2
RTPR
ribonucleoside triphosphate reductase
-
-
-
-
ribonucleotide reductase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2'-deoxyribonucleoside 5'-triphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-triphosphate + thioredoxin
requires a cobamide coenzyme and ATP
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
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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).
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CAS REGISTRY NUMBER
COMMENTARY
9068-66-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
ribonucleoside triphosphate + reduced thioredoxin
-
-
-
-
r
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
ribonucleoside triphosphate + 2-hydroxyethyl disulfide
2'-deoxyribonucleoside triphosphate + 2-mercaptoethanol + H2O
-
-
-
-
?
ribonucleoside triphosphate + dihydrolipoate
2'-deoxyribonucleoside triphosphate + lipoate + H2O
ribonucleoside triphosphate + dithioerythritol
2'-deoxyribonucleoside triphosphate + ? + H2O
ribonucleoside triphosphate + dithiothreitol
2'-deoxyribonucleoside triphosphate + ? + H2O
ribonucleoside triphosphate + NADP+
2'-deoxyribonucleoside triphosphate + NADPH + H2O
-
-
-
-
?
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
ribonucleoside triphosphate + reduced thioredoxin
deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
ribonucleoside triphosphate + thioredoxin
2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H2O
-
-
-
-
?
ADP + reduced thioredoxin
dADP + oxidized thioredoxin + H2O
-
-
-
-
?
ADP + reduced thioredoxin
dADP + oxidized thioredoxin + H2O
-
-
-
-
?
ADP + reduced thioredoxin
dADP + oxidized thioredoxin + H2O
-
most active diphosphate substrate
-
-
?
ATP + reduced thioredoxin
dATP + oxidized thioredoxin + H2O
-
-
-
-
?
ATP + reduced thioredoxin
dATP + oxidized thioredoxin + H2O
-
-
-
-
?
ATP + reduced thioredoxin
dATP + oxidized thioredoxin + H2O
-
-
-
-
?
CDP + reduced dithiothreitol
dCDP + oxidized dithiothreitol + H2O
-
-
-
-
r
CDP + reduced dithiothreitol
dCDP + oxidized dithiothreitol + H2O
-
-
-
-
?
CDP + reduced dithiothreitol
dCDP + oxidized dithiothreitol + H2O
Priestia megaterium KM / ATCC 13632
-
-
-
-
?
CDP + reduced thioredoxin
dCDP + oxidized thioredoxin + H2O
-
-
-
-
?
CDP + reduced thioredoxin
dCDP + oxidized thioredoxin + H2O
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
-
?
CDP + reduced thioredoxin
dCDP + oxidized thioredoxin + H2O
-
-
-
-
?
CDP + reduced thioredoxin
dCDP + oxidized thioredoxin + H2O
-
-
-
-
?
CDP + reduced thioredoxin
dCDP + oxidized thioredoxin + H2O
-
poorly reduced
-
-
?
CDP + reduced thioredoxin
dCDP + oxidized thioredoxin + H2O
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
-
?
CMP + reduced thioredoxin
dCMP + oxidized thioredoxin + H2O
-
-
-
-
?
CMP + reduced thioredoxin
dCMP + oxidized thioredoxin + H2O
-
poorly reduced
-
-
?
CTP + reduced thioredoxin
dCTP + oxidized thioredoxin + H2O
-
-
-
-
?
CTP + reduced thioredoxin
dCTP + oxidized thioredoxin + H2O
-
-
-
-
?
CTP + reduced thioredoxin
dCTP + oxidized thioredoxin + H2O
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
-
?
CTP + reduced thioredoxin
dCTP + oxidized thioredoxin + H2O
-
-
-
-
?
CTP + reduced thioredoxin
dCTP + oxidized thioredoxin + H2O
-
-
-
-
?
CTP + reduced thioredoxin
dCTP + oxidized thioredoxin + H2O
-
-
-
?
CTP + reduced thioredoxin
dCTP + oxidized thioredoxin + H2O
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
-
?
CTP + reduced thioredoxin
dCTP + thioredoxin disulfide + H2O
-
-
-
-
?
CTP + reduced thioredoxin
dCTP + thioredoxin disulfide + H2O
-
-
-
-
?
GDP + reduced thioredoxin
dGDP + oxidized thioredoxin + H2O
-
-
-
-
?
GDP + reduced thioredoxin
dGDP + oxidized thioredoxin + H2O
-
poorly reduced
-
-
?
GTP + reduced thioredoxin
dGTP + oxidized thioredoxin + H2O
-
-
-
-
?
GTP + reduced thioredoxin
dGTP + oxidized thioredoxin + H2O
-
-
-
-
?
GTP + reduced thioredoxin
dGTP + oxidized thioredoxin + H2O
-
-
-
-
?
nucleoside 5'-triphosphate + formate
2'-deoxynucleoside 5'-triphosphate + H2O
-
class III RNR
-
-
?
nucleoside 5'-triphosphate + formate
2'-deoxynucleoside 5'-triphosphate + H2O
Tequatrovirus T4
-
class III RNR
-
-
?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
class II RNRs
-
-
?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
class III RNR
-
-
?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
class II RNRs
-
-
?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
class III RNR
-
-
?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
class III RNR
-
-
?
ribonucleoside triphosphate + dihydrolipoate
2'-deoxyribonucleoside triphosphate + lipoate + H2O
-
-
-
-
?
ribonucleoside triphosphate + dihydrolipoate
2'-deoxyribonucleoside triphosphate + lipoate + H2O
-
-
-
-
?
ribonucleoside triphosphate + dihydrolipoate
2'-deoxyribonucleoside triphosphate + lipoate + H2O
-
-
-
-
?
ribonucleoside triphosphate + dithioerythritol
2'-deoxyribonucleoside triphosphate + ? + H2O
-
-
-
-
?
ribonucleoside triphosphate + dithioerythritol
2'-deoxyribonucleoside triphosphate + ? + H2O
-
-
-
-
?
ribonucleoside triphosphate + dithioerythritol
2'-deoxyribonucleoside triphosphate + ? + H2O
-
-
-
-
?
ribonucleoside triphosphate + dithioerythritol
2'-deoxyribonucleoside triphosphate + ? + H2O
-
-
-
-
?
ribonucleoside triphosphate + dithiothreitol
2'-deoxyribonucleoside triphosphate + ? + H2O
-
-
-
-
?
ribonucleoside triphosphate + dithiothreitol
2'-deoxyribonucleoside triphosphate + ? + H2O
-
-
-
-
?
ribonucleoside triphosphate + dithiothreitol
2'-deoxyribonucleoside triphosphate + ? + H2O
-
-
-
-
?
ribonucleoside triphosphate + GSSG
2'-deoxyribonucleoside triphosphate + GSH + H2O
-
-
-
-
?
ribonucleoside triphosphate + GSSG
2'-deoxyribonucleoside triphosphate + GSH + H2O
-
-
-
-
?
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
Astasia sp.
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
437887, 437888, 437889, 437890, 437891, 437892, 437893, 437894, 437896, 437897, 437898, 437899, 437900, 437901, 437902, 437903
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin
deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
Astasia sp.
-
-
-
-
?
ribonucleoside triphosphate + reduced thioredoxin
deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
?
ribonucleoside triphosphate + reduced thioredoxin
deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
?
ribonucleoside triphosphate + reduced thioredoxin
deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
?
ribonucleoside triphosphate + reduced thioredoxin
deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
?
ribonucleoside triphosphate + reduced thioredoxin
deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
?
ribonucleoside triphosphate + reduced thioredoxin
deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
?
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
Astasia sp.
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
key enzyme in the pathway of DNA biosynthesis in all organisms
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
437887, 437889, 437890, 437891, 437892, 437893, 437894, 437896, 437897, 437898, 437899, 437901, 437902, 437903
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
physiological hydrogen donor is unknown
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
catalyzes the rate-determining step in DNA biosynthesis
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
UDP + reduced thioredoxin
dUDP + oxidized thioredoxin + H2O
-
-
-
-
?
UDP + reduced thioredoxin
dUDP + oxidized thioredoxin + H2O
-
poorly reduced
-
-
?
UTP + reduced thioredoxin
dUTP + oxidized thioredoxin + H2O
-
-
-
-
?
UTP + reduced thioredoxin
dUTP + oxidized thioredoxin + H2O
-
-
-
-
?
UTP + reduced thioredoxin
dUTP + oxidized thioredoxin + H2O
-
-
-
-
?
additional information
?
-
the small subunit of RNR2 interacts in planta with the C-terminal section of signalosome protein complex COP9 subunit 7, CSN7, overview
-
-
?
additional information
?
-
the small subunit of RNR2 interacts in planta with the C-terminal section of signalosome protein complex COP9 subunit 7, CSN7, overview
-
-
?
additional information
?
-
the small subunit of RNR2 interacts in planta with the C-terminal section of signalosome protein complex COP9 subunit 7, CSN7, overview
-
-
?
additional information
?
-
the small subunit of RNR2 interacts in planta with the C-terminal section of signalosome protein complex COP9 subunit 7, CSN7, overview
-
-
?
additional information
?
-
-
class II RNRs convert nucleoside triphosphates and nucleoside 5'-diphosphates, see also EC 1.17.4.1, to the correspondent 2'-deoxy products, overview
-
-
?
additional information
?
-
-
In class II a tyrosine radical is generated directly on alpha or alpha2 by cleavage of adenosylcobalamin. In class III a glycyl radical is generated on alpha2 when a radical SAM protein cleaves S-adenosylmethionine. In both cases, the radical is channeled to a cysteine in the active site of the alpha subunit to initiate catalysis
-
-
?
additional information
?
-
-
the class II RNR also uses nucleoside 5'-diphosphate as substrate
-
-
?
additional information
?
-
-
the anaerobic ribonucleotide reductase of Escherichia coli is an essential enzyme required to supply the building blocks for DNA synthesis
-
-
?
additional information
?
-
-
p53-dependent small enzyme subunit M2B may play an important role for initiating DNA replication in normal growth
-
-
?
additional information
?
-
-
the enzyme produces deoxyribonucleotide triphosphates, dNTPs
-
-
?
additional information
?
-
-
the enzyme also catalyzes the exchange of the C5'-hydrogens of adenosylcobalamin with solvent hydrogen, epimerization of the (5'S)-[5'-2H1]- and (5'R)-[5'-2H1]-isotopomers of adenosylcobalamin
-
-
?
additional information
?
-
-
RTPR catalyzes the conversion of nucleoside triphosphates to deoxynucleotides requiring adenosylcobalamin as a cofactor, model of reaction mechanism, overview
-
-
?
additional information
?
-
-
RTPR catalyzes the conversion of nucleoside triphosphates to deoxynucleotides using adenosylcobalamin as a cofactor
-
-
?
additional information
?
-
-
class II RNRs convert nucleoside triphosphates and nucleoside 5'-diphosphates, see also EC 1.17.4.1, to the correspondent 2'deoxy products, overview
-
-
?
additional information
?
-
-
the class II RNR also uses nucleoside 5'-diphosphate as substrate
-
-
?
additional information
?
-
-
the two-component class II RNR is primarily used for DNA repair and/or possibly DNA replication at low oxygen tension. It can support bacterial growth in the absence of class I RNR activity
-
-
?
additional information
?
-
-
In class II a tyrosine radical is generated directly on alpha or alpha2 by cleavage of adenosylcobalamin. In class III a glycyl radical is generated on alpha2 when a radical SAM protein cleaves S-adenosylmethionine. In both cases, the radical is channeled to a cysteine in the active site of the alpha subunit to initiate catalysis
-
-
?
additional information
?
-
-
In class II a tyrosine radical is generated directly on alpha or alpha2 by cleavage of adenosylcobalamin. In class III a glycyl radical is generated on alpha2 when a radical SAM protein cleaves S-adenosylmethionine. In both cases, the radical is channeled to a cysteine in the active site of the alpha subunit to initiate catalysis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
ribonucleoside triphosphate + reduced thioredoxin
-
-
-
-
r
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
ribonucleoside triphosphate + thioredoxin
2'-deoxyribonucleoside triphosphate + thioredoxin disulfide + H2O
-
-
-
-
?
nucleoside 5'-triphosphate + formate
2'-deoxynucleoside 5'-triphosphate + H2O
-
class III RNR
-
-
?
nucleoside 5'-triphosphate + formate
2'-deoxynucleoside 5'-triphosphate + H2O
Tequatrovirus T4
-
class III RNR
-
-
?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
class II RNRs
-
-
?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
class III RNR
-
-
?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
class II RNRs
-
-
?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
class III RNR
-
-
?
nucleoside 5'-triphosphate + thioredoxin
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
class III RNR
-
-
?
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
Astasia sp.
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
key enzyme in the pathway of DNA biosynthesis in all organisms
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
437887, 437889, 437890, 437891, 437892, 437893, 437894, 437896, 437897, 437898, 437899, 437901, 437902, 437903
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
physiological hydrogen donor is unknown
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
catalyzes the rate-determining step in DNA biosynthesis
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
ribonucleoside triphosphate + reduced thioredoxin + H2O
2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H2O
-
-
-
-
r
additional information
?
-
the small subunit of RNR2 interacts in planta with the C-terminal section of signalosome protein complex COP9 subunit 7, CSN7, overview
-
-
?
additional information
?
-
the small subunit of RNR2 interacts in planta with the C-terminal section of signalosome protein complex COP9 subunit 7, CSN7, overview
-
-
?
additional information
?
-
the small subunit of RNR2 interacts in planta with the C-terminal section of signalosome protein complex COP9 subunit 7, CSN7, overview
-
-
?
additional information
?
-
the small subunit of RNR2 interacts in planta with the C-terminal section of signalosome protein complex COP9 subunit 7, CSN7, overview
-
-
?
additional information
?
-
-
class II RNRs convert nucleoside triphosphates and nucleoside 5'-diphosphates, see also EC 1.17.4.1, to the correspondent 2'-deoxy products, overview
-
-
?
additional information
?
-
-
the anaerobic ribonucleotide reductase of Escherichia coli is an essential enzyme required to supply the building blocks for DNA synthesis
-
-
?
additional information
?
-
-
p53-dependent small enzyme subunit M2B may play an important role for initiating DNA replication in normal growth
-
-
?
additional information
?
-
-
the enzyme produces deoxyribonucleotide triphosphates, dNTPs
-
-
?
additional information
?
-
-
RTPR catalyzes the conversion of nucleoside triphosphates to deoxynucleotides requiring adenosylcobalamin as a cofactor, model of reaction mechanism, overview
-
-
?
additional information
?
-
-
RTPR catalyzes the conversion of nucleoside triphosphates to deoxynucleotides using adenosylcobalamin as a cofactor
-
-
?
additional information
?
-
-
class II RNRs convert nucleoside triphosphates and nucleoside 5'-diphosphates, see also EC 1.17.4.1, to the correspondent 2'deoxy products, overview
-
-
?
additional information
?
-
-
the two-component class II RNR is primarily used for DNA repair and/or possibly DNA replication at low oxygen tension. It can support bacterial growth in the absence of class I RNR activity
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
adenosylcobalamin
in the course of catalysis, the protein active site presents the reacting molecules with an environment that includes a hydrogen bond to the thiyl radical and intervening residues or solvent mediating an exchange coupling between the thiyl radical and cob(II)alamin
coenzyme B12
-
adenosylcobalamin
additional information
-
cofactor specificity and binding, role in reaction, overview
-
additional information
-
cofactor specificity and binding, role in reaction, overview
-
additional information
-
the class III enzymes contain 4Fe-4S clusters in the small beta-subunit. Cofactor specificity and binding, role in reaction, overview
-
additional information
Tequatrovirus T4
-
the class III enzymes contain 4Fe-4S clusters in the small beta-subunit. Cofactor specificity and binding, role in reaction, overview
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
Mg2+
Co2+
-
enzyme requires adenosylcobalamin as a cofactor, the Co ion is involved in the reaction
Fe2+
-
the class III enzymes contain 4Fe-4S clusters in the small beta-subunit
Fe2+
Tequatrovirus T4
-
the class III enzymes contain 4Fe-4S clusters in the small beta-subunit
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,3',4,4',5,5'-hexahydroxy-trans-stilbene
-
i.e. M8, a resveratrol analogue, inhibits the enzyme and causes an imbalance of intracellular dNTP pools, the dATP pool is eliminated, while the dCTP and dTTP pools are enlarged. M8 leads to complete growth inhibition of HT-29 cells at 0.015 mM within 7 days, overview
3-aminopyridine-2-carboxaldehyde thiosemicarbazone
-
i.e.3-AP or triapine, in combination with the nucleoside analog fludarabine for patients with refractory acute leukemias and aggressive myeloprol, phase I study, detailed overview, the inhibitor inhibits the M2 subunit, and depletes intracellular deoxyribonculeotide pools, especially dATP
3-aminopyridine-2-carboxaldehyde-thiosemicarbazone
-
i.e. 3-AP, phase I study in combination with high dose cytarabine in patients with advanced myeloid leukemia, resulting in enhanced cytarabine cytotoxicity with possible methemoglobinemia, overview
gallic acid
-
inhibition of enzyme activity and induction of dose-dependent apoptosis and attenuated progression from G0/G1 to S phase of cells cycle. Highly synergistic effects of simultaneous treatment of cells with gallic acid and enzyme inhibitor N',3,4,5-tetrahydroxybenzenecarboximidamide
IRBIT
-
IRBIT is a conserved metazoan protein implicated in diverse functions. IRBIT consists of a putative enzymatic domain that has similarity to S-adenosylhomocysteine hydrolase and an essential N-terminal domain of 104 amino acids. It forms a dATP-dependent complex with ribonucleotide reductase, which stabilizes dATP in the activity site of ribonucleotide reductase and thus inhibits the enzyme. Formation of the ribonucleotide reductase-IRBIT complex is regulated through phosphorylation of IRBIT, and ablation of IRBIT expression in HeLa cells causes imbalanced dNTP pools and altered cell cycle progression. Under normal physiological conditions, where ATP levels are high, such inhibition can only be achieved when binding of IRBIT is strengthened by phosphorylation
-
N',3,4,5-tetrahydroxybenzenecarboximidamide
-
i.e. trimidox, highly synergistic effects of simultaneous treatment of cells with inhibitors gallic acid and trimidox
N-hydroxy-N'-(3,4,5-trimethoxyphenyl)-3,4,5-trimethoxybenzamidine
-
a resveratrol analogue, inhibits the enzyme in HL-60 cells showing synergistic effects with arabinofuranosylcytosine in antitumor activity, overview
signalosome protein complex COP9
i.e. CSN, is a negative regulator of RNR2 activity in Arabidopsis thaliana. The pleiotropic regulator of plant development and contains eight-subunits, RNR2 binds to the C-terminus of subunit 7, CSN7; i.e. CSN, is a negative regulator of RNR2 activity in Arabidopsis thaliana. The pleiotropic regulator of plant development and contains eight-subunits, RNR2 binds to the C-terminus of subunit 7, CSN7
-
2',2'-difluoro-2'-deoxycytidine 5'-triphosphate
-
complete inactivation of the enzyme by 1 equiv of 2',2'-difluoro-2'-deoxyCTP, F2CTP, in about 2 min proceeding via alkylation by the sugar of F2CTP and AdoCbl destruction. 0.47 equiv of a sugar moiety is covalently bound to RNR and 0.25 equiv of a cobalt(III) corrin is tightly associated, likely through a covalent interaction with C419 (Co-S) in the active site of RNR. Analysis of the relationship of the nonalkylative pathway for RNR inactivation relative to the alkylative pathway, overview
2',2'-difluoro-2'-deoxycytidine 5'-triphosphate
-
F2CTP, a clinically used anti-cancer drug, synthesis, overview. Causes rapid enzyme inactivation through covalent modification, mechanism of inactivation, analysis by mass spectrometry and radio- or deuterium-labeled compounds, overview. C119 is involved in the reaction
dTTP
-
inhibits CTP, ATP and GTP reduction, reduction of UTP is unaffected by deoxyribonucleotides
gemcitabine
-
i.e. 2',2'-difluoro-2'-deoxycytidine, dFdC, a deoxycytidine analogue, very active drug against solid tumors, the RNR inactivation is reductant-dependent for R1 subunit, but reductant-independent for the R2 subunit, R1 inactivation is the most favorable mechanism responsible for the drug's cytotoxicity, overview, binding and inhibition mechanism including the formation of a Cys225-Cys462 disulfide bridge, detailed overview
triapine
-
i.e. 3-AP, triapine enhances the cytotoxicity of gemcitabine and arabinoside cytosine in four non-small-cell-lung-cancer cell lines, e.g. in SW1573 cells, but not in H460 cells, multiple-drug-effect analysis, overview
triapine
-
a potent ribonucleotide reductase inhibitor, phase I and pharmacokinetic study in adults with advanced hematologic malignancies, detailed overview
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dGTP
-
both epimerization and 5'-hydrogen exchange reactions are stimulated by the allosteric effector
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetics with gemcitabine
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
adults with refractory acute leukemias and aggressive myeloproliferative disorders, MPD
-
-
brenda
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437888, 437889, 437891, 437893, 437894, 437896, 437897, 437898, 437900, 437901, 437902, 437903, 657991, 714185, 714186
-
-
brenda
mutant of strain ATCC 4797, produced during many years of transfers on litmus milk
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-
brenda
serovar Typhimurium, inside RAW264.7 macrophages or HeLa cells
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
fibroblast cell, non-dividing cells expressing enzyme subunit p53R2, but not sunit R2 protein, have reduced dNTP levels if exposed to the enzyme--specific inhibitor hydroxyurea. After DNA damage, a slow, up to 4fold increase in p53R2 expression leads to 3fold increase in dNTP pools in G0/G1 cells
brenda
-
colon cancer cell. Cell line expresses subunit R2 in excess resulting in protection against DNA damage and replication stress
brenda
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oropharyngeal epidermal carcinoma cell line. At G1/S phase transition, level of p53-dependent small enzyme subunit M2B increases to maximum levles, and decreases with DNA synthesis. In response to DNA replication, subunit M2B redistributes from the cytoplasm to the nucleus earlier than small subunit M2
brenda
-
higest expression of subunit R2 in ovary of blood-fed or sugar-fed animals. Significant induction following blood feeding
brenda
additional information
additional information
-
expression of subunit isoform RNR2B in all tissues tested, but at low level
brenda
additional information
expression of subunit isoform RNR2B in all tissues tested, but at low level
brenda
additional information
RNR2Tso2 is more prevalent than RNR2A throughout development and in most organs, suggesting that RNR2Tso2 is the predominant RNR2 in Arabidopsis thaliana. RNR2Tso2 levels are more varied than RNR2A levels in response to environmental changes and exposure to chemicals
brenda
additional information
RNR2Tso2 is more prevalent than RNR2A throughout development and in most organs, suggesting that RNR2Tso2 is the predominant RNR2 in Arabidopsis thaliana. RNR2Tso2 levels are more varied than RNR2A levels in response to environmental changes and exposure to chemicals
brenda
additional information
-
RNR2Tso2 is more prevalent than RNR2A throughout development and in most organs, suggesting that RNR2Tso2 is the predominant RNR2 in Arabidopsis thaliana. RNR2Tso2 levels are more varied than RNR2A levels in response to environmental changes and exposure to chemicals
-
brenda
additional information
-
RNR expression in small cell lung cancer cell lines, overview
brenda
additional information
-
exponentialy grown cells predominantly express class I enzyme compared with class II enzyme, activity in stationary phase cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
the subcellular localization of RNR2 is primarily nuclear in meristematic regions, and cytoplasmic in adult cells. RNR2 is constitutively nuclear in csn7 mutant seedlings
brenda
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the subcellular localization of RNR2 is primarily nuclear in meristematic regions, and cytoplasmic in adult cells. RNR2 is constitutively nuclear in csn7 mutant seedlings
-
brenda
-
in response to DNA replication, subunit M2B redistributes from the cytoplasm to the nucleus
brenda
the subcellular localization of RNR2 is primarily nuclear in meristematic regions, and cytoplasmic in adult cells. RNR2 is constitutively nuclear in csn7 mutant seedlings
brenda
-
the subcellular localization of RNR2 is primarily nuclear in meristematic regions, and cytoplasmic in adult cells. RNR2 is constitutively nuclear in csn7 mutant seedlings
-
brenda
-
in response to DNA replication, subunit M2B redistributes from the cytoplasm to the nucleus
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
RNR is the rate-limiting enzyme in deoxyribonucleoside triphosphate, dNTP, biosynthesis
physiological function
additional information
physiological function
-
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
additional information
-
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
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000
69300
-
enzyme in 6 M guanidine-HCl, 0.1 M dithiothreitol, equilibrium ultracentrifugation
72500
-
native enzyme in 0.1 M glycine buffer, pH 9.1, equilibrium ultracentrifugation
72600
-
maleated enzyme in 0.05 M phosphate buffer, equilibrium ultracentrifugation
74500
-
enzyme in 6 M guanidine-HCl, 0.1 M dithiothreitol, heated for 20 min at 60°C, equilibrium ultracentrifugation
75300
-
native enzyme in 0.05 M phosphate buffer, pH 7.0, sedimentation equilibrium method
76000
81850
-
predicted molecular weight based on the predicted amino acid sequence from the sequenced gene
90000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
monomer or dimer
tetramer
additional information
tetramer
-
alpha2beta2 heterodimer with a regulatory, nucleotide binding site M1 subunit, and an inducible, catalytic M2 subunit which contains non-heme iron and a tyrosyl free radical, that are required for the enzymatic reduction of ribonucleotides
tetramer
-
RNR is a tetramer consisting of two non-identical homodimers. The two identical M2 subunits regulate the substrate specificity of the enzyme, while the other two identical M1 subunits are responsible for the activity by binding the ribonucleotides and allosteric effectors
additional information
-
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
additional information
-
structures of the active holoenzymes of class I-III RNRs, structure comparisons, overview
additional information
-
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
additional information
-
the enzyme is encoded by two consecutive open reading frames denated nrdJa and nrdJb and separated by 16 bp. The presence of both NrdJa and NrdJb subunits is absolutely essential for enzyme activity
additional information
-
structures of the active holoenzymes of class I-III RNRs, structure comparisons, overview
additional information
-
structures of the active holoenzymes of class I-III RNRs, structure comparisons, overview
additional information
Tequatrovirus T4
-
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure alone and in several complexes, including with the allosteric effector dATP and its cognate substrate CTP
enzyme in complex with dATP, DTTP, dGTP, dTTP-GDP, dGTP-ADP, dATP-CDP or dATP-UDP
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C408A
-
only wild-type enzyme catalyzes epimerization of the (5'S)-[5'-2H1]- and (5'R)-[5'-2H1]-isotopomers of adenosylcobalamin, no activity of mutant enzyme
C408S
-
only wild-type enzyme catalyzes epimerization of the (5'S)-[5'-2H1]- and (5'R)-[5'-2H1]-isotopomers of adenosylcobalamin, no activity of mutant enzyme
additional information
additional information
-
mutants in subunit R2 isoform tso2 show reduced deoxyribonucleotide triphosphate levels and developmental defects including callus-like floral organs and fasciated shoot apical stems. R2 isoforms tso2 single and tso2/rnr2a double mutants are more sensitive to UV-C light and double mutant seedlings exhibit increased DNA damage, massive programmed cell death, and release of transcriptional gene silencing
additional information
mutants in subunit R2 isoform tso2 show reduced deoxyribonucleotide triphosphate levels and developmental defects including callus-like floral organs and fasciated shoot apical stems. R2 isoforms tso2 single and tso2/rnr2a double mutants are more sensitive to UV-C light and double mutant seedlings exhibit increased DNA damage, massive programmed cell death, and release of transcriptional gene silencing
additional information
-
mutation cls8, i.e. crinkled leaves8, is a mutant of the large subunit R1 of ribonucleotide reductase. the mutation leads to abnormal leaf and flower morphology, reduced root growth and bleache leaf sections. Levels of dTTP and dATP are significantly reduced
additional information
construction of two T-DNA insertion mutants of the RNR2Tso2, inserted within the coding sequence of the second exon of RNR2Tso2. No plants homozygous for the T-DNA allele are detectable for either allele
additional information
construction of two T-DNA insertion mutants of the RNR2Tso2, inserted within the coding sequence of the second exon of RNR2Tso2. No plants homozygous for the T-DNA allele are detectable for either allele
additional information
-
construction of two T-DNA insertion mutants of the RNR2Tso2, inserted within the coding sequence of the second exon of RNR2Tso2. No plants homozygous for the T-DNA allele are detectable for either allele
-
additional information
-
fnr and arcA mutant strains are constructed by introducing the indicated mutation into strain IG40 by P1 transduction followed by selection for the appropriate drug resistance
additional information
-
in p53null cells, siRNA-mediated knockdown of about 80% of R2 subunits has no effect on proliferative growth but results in enhanced accumulation of gamma-H2Ax and delayed recovery from DNA lesions inflicted by exposure to cisplatin and Triapine. Level of R1 subunits is limiting since depletion of the R1 subunit directly activates the S phase checkpoint due to replication stress
additional information
-
isolation of a p53R2 mutant from skin fibroblasts, quiescent p53R2 mutant cells contain more isozyme R2, incorporate more BrdU into cell nuclei, and synthesize more DNA from dTMP than matched controls
additional information
-
generation of RNR transgenic mice expressing one or more subunits of RNR, phenotypes, overview
additional information
-
cell lacking thioredoxins exhibit an elongated S phase and accumulate subunit R1 in its oxidized form. Cells also contain significantly decreased deoxyribonucleotide levels during the S phase. Overexpressing subunit R1 in these cells increases both the amount of R1 reduced form and the concentrations of deoxyribonucleotides and accelerates DNA replication
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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
-
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-100°C, may be stored as frozen paste for at least 3 months without significant loss of activity
-
-20°C, crude extracts relatively unstable, most of the activity disappears within a few weeks
-
-65°C, no detectable loss of enzyme has been observed during several years of storage of packed bacteria
-
0-4°C, acetone and hydroxylapatite fractions are quite stable, at least 70-80% of their activities remain after 3 months
-
0-4°C, crude extracts relatively unstable, most of the activity disappears within a few weeks
-
20°C, 0.03 M dimethylglutarate buffer, pH 7.2, remains fully active on storage for 24 h
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant RNR2 from transgenic Arabidopsis thaliana plants by affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chromosomal DNA containg RNR gene PCR amplified, gene cloned, completely sequenced and expressed in Escherichia coli
-
cloned by PCR from peptide sequence information, nrdj gene sequenced completely and expressed in Escherichia coli BL21(DE3)
-
high-level overexpression of RNR subunits, Rrm1, Rrm2 and p53R2, separately or in different combinations, in mice, simultaneous expression of two RNR subunits
-
the nrdDG promoter regulates transcriptional expression of the anaerobic ribonucleotide reductase of Escherichia coli, binding of the pleiotropic FNR, fumarate and nitrate reduction, transcriptional regulator to the nrdDG promoter region affects the transcription, the upstream FNR-2 site is essential for anaerobic activation of the nrdDG promoter. Although the FNR-1 site is not absolutely required, it allows maximal expression of this promoter, overview
-
two-hybrid interaction analysis of CSN7 and RNR2 expressing the vectors under control of the 35S promoter in Nicotiana benthamiana cells, transgenic expression of RNR2 in Arabidopsis thaliana plants
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
endogenous RNR transcripts are downregulated in response to large increases of mtDNA in mice, which is indicative of nuclear-mitochondrial crosstalk with regard to mtDNA copy number
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
development of a rapid freeze-quench apparatus for the preparation of millisecond quench time rapid freeze-quench samples which can be packed into small sample tubes used for continuous-wave and pulsed high-frequency electron paramagnetic resonance spectroscopy
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bakley, R.L.
Cobamides and ribonucleotide reduction. I. Cobamide stimulation of ribonucleotide reduction in extracts of Lactobacillus leichmannii
J. Biol. Chem.
240
2173-2180
1965
Lactobacillus leichmannii
brenda
Goulian, M.; Beck, W.S.
Purification and properties of cobamide-dependent ribonucleotide reductase from Lactobacillus leichmannii
J. Biol. Chem.
241
4233-4242
1966
Lactobacillus leichmannii
brenda
Sando, G.N.; Hogenkamp, H.P.C.
Ribonucleotide reductase from Thermus X-1, a thermophilic organism
Biochemistry
12
3316-3322
1973
Lactobacillus leichmannii, Thermus aquaticus, Thermus sp., Thermus sp. X-1, Thermus aquaticus YT-1
brenda
Chen, A.K.; Bhan, A.; Hopper, S.; Abrams, R.; Franzen, J.S.
Substrate and effector binding to ribonucleoside triphosphate reductase of Lactobacillus leichmannii
Biochemistry
13
654-661
1974
Lactobacillus leichmannii
brenda
Hamilton, F.D.
Ribonucleotide reductase from Euglena gracilis. A 5-deoxyadenoslycobalamin-dependent enzyme
J. Biol. Chem.
249
4428-4434
1974
Escherichia coli, Euglena gracilis, Lactobacillus leichmannii, Euglena gracilis Z
brenda
Blakley, R.L.
Ribonucleoside triphosphate reductase from Lactobacillus leichmannii
Methods Enzymol.
51
246-259
1978
Astasia sp., Clostridium sp., Corynebacterium sp., Euglena sp., Lactobacillus leichmannii, Pseudomonas sp., Rhizobium sp.
brenda
Gleason, F.K.; Frick, T.D.
Adenosylcobalamin-dependent ribonucleotide reductase from the blue-green alga, Anabaena sp. Purification and partial characterization
J. Biol. Chem.
255
7728-7733
1980
Anabaena sp., Escherichia coli, Lactobacillus leichmannii, Anabaena sp. 7119
brenda
Ashley, G.W.; Harris, G.; Stubbe, J.
The mechanism of Lactobacillus leichmannii ribonucleotide reductase. Evidence for 3 carbon-hydrogen bond cleavage and a unique role for coenzyme B12
J. Biol. Chem.
261
3958-3964
1986
Lactobacillus leichmannii
brenda
Halicky, P.; Kollarova, M.; Kois, P.; Zelinka, J.
Immobilization of ribonucleotide reductase from Streptomyces aureofaciens
Collect. Czech. Chem. Commun.
54
2528-2541
1989
Kitasatospora aureofaciens
brenda
Booker, S.; Licht, S.; Broderick, J.; Stubbe, J.
Coenzyme B12-dependent ribonucleotide reductase: evidence for the participation of five cysteine residues in ribonucleotide reduction
Biochemistry
33
12676-12685
1994
Lactobacillus leichmannii
brenda
Jordan, A.; Torrents, E.; Jeanthon, C.; Eliasson, R.; Hellman, U.; Wernstedt, C.; Barbe, J.; Gibert, I.; Reichard, P.
B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli
Proc. Natl. Acad. Sci. USA
94
13487-13492
1997
Archaeoglobus fulgidus, Chloroflexus aurantiacus, Deinococcus radiodurans, Escherichia coli, Lactobacillus leichmannii, Methanocaldococcus jannaschii, Mycobacterium tuberculosis, Pyrococcus furiosus, Thermoplasma acidophilum, Thermotoga maritima, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
brenda
Tauer, A.; Benner, S.A.
The B12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: an evolutionary solution to the ribonucleotide reductase conundrum
Proc. Natl. Acad. Sci. USA
94
53-58
1997
Anabaena sp., Escherichia coli, Halobacterium salinarum, Haloferax volcanii, Homo sapiens, Lactobacillus leichmannii, Mycobacterium tuberculosis, Thermoplasma acidophilum, Thermus aquaticus, Thermus aquaticus X1
brenda
Jordan, A.; Torrents, E.; Sala, I.; Hellman, U.; Gibert, I.; Reichard, P.
Ribonucleotide reduction in Pseudomonas species: simultaneous presence of active enzymes from different classes
J. Bacteriol.
181
3974-3980
1999
Brevundimonas diminuta, Brevundimonas vesicularis, Burkholderia cepacia, Delftia acidovorans, Deinococcus radiodurans, Escherichia coli, Hydrogenophaga flava, Lactobacillus leichmannii, Paracoccus denitrificans, Mycobacterium tuberculosis, Pseudomonas sp., Pseudomonas aeruginosa, Pseudomonas putida, Stenotrophomonas maltophilia, Pseudomonas stutzeri, Ralstonia pickettii, Xanthomonas campestris
brenda
Licht, S.S.; Booker, S.; Stubbe, J.
Studies on the catalysis of carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: evidence for concerted carbon-cobalt bond homolysis and thiyl radical formation
Biochemistry
38
1221-1233
1999
Escherichia coli, Lactobacillus leichmannii
brenda
Licht, S.S.; Lawrence, C.C.; Stubbe, J.
Thermodynamic and kinetic studies on carbon-cobalt bond homolysis by ribonucleoside triphosphate reductase: The importance of entropy in catalysis
Biochemistry
38
1234-1242
1999
Lactobacillus leichmannii
brenda
Suto, R.K.; Poppe, L.; Retey, J.; Finke, R.G.
Ribonucleoside triphosphate reductase from Lactobacillus leichmannii: Kinetic evaluation of a series of adenosylcobalamin competitive inhibitors, [omega-(adenosin-5'-O-yl)alkyl]cobalamins, which mimic the post Co-C homolysis intermediate
Bioorg. Chem.
27
451-462
1999
Lactobacillus leichmannii
-
brenda
Suto, R.K.; Whalen, M.A.; Finke, R.G.
Adenosylcobalamin-dependent ribonucleoside triphosphate reductase from Lactobacillus leichmannii. Rapid, improved purification involving dGTP-based affinity chromatography plus biophysical characterization studies demonstrating enhanced, crystallographic level purity
Prep. Biochem. Biotechnol.
29
273-309
1999
Lactobacillus leichmannii
brenda
Chabes, A.; Domkin, V.; Larsson, G.; Liu, A.; Graslund, A.; Wijmenga, S.; Thelander, L.
Yeast ribonucleotide reductase has a heterodimeric iron-radical-containing subunit
Proc. Natl. Acad. Sci. USA
97
2474-2479
2000
Saccharomyces cerevisiae
brenda
Hoegbom, M.; Huque, Y.; Sjoeberg, B.M.; Nordlund, P.
Crystal structure of the di-iron/radical protein of ribonucleotide reductase from Corynebacterium ammoniagenes
Biochemistry
41
1381-1389
2002
Corynebacterium ammoniagenes
brenda
Chen, D.; Abend, A.; Stubbe, J.; Frey, P.A.
Epimerization at carbon-5' of (5'R)-[5'-2H]adenosylcobalamin by ribonucleoside triphosphate reductase: cysteine 408-independent cleavage of the Co-C5'-bond
Biochemistry
42
4578-4584
2003
Lactobacillus leichmannii
brenda
Torrents, E.; Poplawski, A.; Sjoberg, B.M.
Two proteins mediate class II ribonucleotide reductase activity in Pseudomonas aeruginosa: expression and transcriptional analysis of the aerobic enzymes
J. Biol. Chem.
280
16571-16578
2005
Pseudomonas aeruginosa
brenda
Larsson, K.M.; Jordan, A.; Eliasson, R.; Reichard, P.; Logan, D.T.; Nordlund, P.
Structural mechanism of allosteric substrate specificity regulation in a ribonucleotide reductase
Nat. Struct. Mol. Biol.
11
1142-1149
2004
Thermotoga maritima
brenda
Logan, D.T.; Mulliez, E.; Larsson, K.M.; Bodevin, S.; Atta, M.; Garnaud, P.E.; Sjberg, B.M.; Fontecave, M.
A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase
Proc. Natl. Acad. Sci. USA
100
3826-3831
2003
Escherichia coli, Escherichia coli JM109
brenda
Liu, X.; Zhou, B.; Xue, L.; Shih, J.; Tye, K.; Qi, C.; Yen, Y.
The ribonucleotide reductase subunit M2B subcellular localization and functional importance for DNA replication in physiological growth of KB cells
Biochem. Pharmacol.
70
1288-1297
2005
Homo sapiens
brenda
Lin, Z.P.; Belcourt, M.F.; Carbone, R.; Eaton, J.S.; Penketh, P.G.; Shadel, G.S.; Cory, J.G.; Sartorelli, A.C.
Excess ribonucleotide reductase R2 subunits coordinate the S phase checkpoint to facilitate DNA damage repair and recovery from replication stress
Biochem. Pharmacol.
73
760-772
2007
Homo sapiens
brenda
Madlener, S.; Illmer, C.; Horvath, Z.; Saiko, P.; Losert, A.; Herbacek, I.; Grusch, M.; Elford, H.L.; Krupitza, G.; Bernhaus, A.; Fritzer-Szekeres, M.; Szekeres, T.
Gallic acid inhibits ribonucleotide reductase and cyclooxygenases in human HL-60 promyelocytic leukemia cells
Cancer Lett.
245
156-162
2007
Homo sapiens
brenda
Camier, S.; Ma, E.; Leroy, C.; Pruvost, A.; Toledano, M.; Marsolier-Kergoat, M.C.
Visualization of ribonucleotide reductase catalytic oxidation establishes thioredoxins as its major reductants in yeast
Free Radic. Biol. Med.
42
1008-1016
2007
Saccharomyces cerevisiae
brenda
Pham, D.Q.; Kos, P.J.; Mayo, J.J.; Winzerling, J.J.
Regulation of the ribonucleotide reductase small subunit (R2) in the yellow fever mosquito, Aedes aegypti
Gene
372
182-190
2006
Aedes aegypti
brenda
Hakansson, P.; Hofer, A.; Thelander, L.
Regulation of mammalian ribonucleotide reduction and dNTP pools after DNA damage and in resting cells
J. Biol. Chem.
281
7834-7841
2006
Mus musculus
brenda
Wang, C.; Liu, Z.
Arabidopsis ribonucleotide reductases are critical for cell cycle progression, DNA damage repair, and plant development
Plant Cell
18
350-365
2006
Arabidopsis thaliana, Arabidopsis thaliana (P0DKH2)
brenda
Garton, S.; Knight, H.; Warren, G.J.; Knight, M.R.; Thorlby, G.J.
crinkled leaves 8 - A mutation in the large subunit of ribonucleotide reductase - leads to defects in leaf development and chloroplast division in Arabidopsis thaliana
Plant J.
50
118-127
2007
Arabidopsis thaliana
brenda
Yau, S.; Wachsman, J.T.
The Bacillus megaterium ribonucleotide reductase: evidence for a B 12 coenzyme requirement
Mol. Cell. Biochem.
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Priestia megaterium, Priestia megaterium KM / ATCC 13632
brenda
Sigmond, J.; Kamphuis, J.A.; Laan, A.C.; Hoebe, E.K.; Bergman, A.M.; Peters, G.J.
The synergistic interaction of gemcitabine and cytosine arabinoside with the ribonucleotide reductase inhibitor triapine is schedule dependent
Biochem. Pharmacol.
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Homo sapiens
brenda
Cerqueira, N.M.; Fernandes, P.A.; Ramos, M.J.
Understanding ribonucleotide reductase inactivation by gemcitabine
Chemistry
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2007
Escherichia coli
brenda
Saiko, P.; Ozsvar-Kozma, M.; Bernhaus, A.; Jaschke, M.; Graser, G.; Lackner, A.; Grusch, M.; Horvath, Z.; Madlener, S.; Krupitza, G.; Handler, N.; Erker, T.; Jaeger, W.; Fritzer-Szekeres, M.; Szekeres, T.
N-hydroxy-N-(3,4,5-trimethoxyphenyl)-3,4,5-trimethoxy-benzamidine, a novel resveratrol analog, inhibits ribonucleotide reductase in HL-60 human promyelocytic leukemia cells: synergistic antitumor activity with arabinofuranosylcytosine
Int. J. Oncol.
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Homo sapiens
brenda
Roca, I.; Ballana, E.; Panosa, A.; Torrents, E.; Gibert, I.
Fumarate and nitrate reduction (FNR) dependent activation of the Escherichia coli anaerobic ribonucleotide reductase nrdDG promoter
Int. Microbiol.
11
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Escherichia coli K-12
brenda
Odenike, O.M.; Larson, R.A.; Gajria, D.; Dolan, M.E.; Delaney, S.M.; Karrison, T.G.; Ratain, M.J.; Stock, W.
Phase I study of the ribonucleotide reductase inhibitor 3-aminopyridine-2-carboxaldehyde-thiosemicarbazone (3-AP) in combination with high dose cytarabine in patients with advanced myeloid leukemia
Invest. New Drugs
26
233-239
2008
Homo sapiens
brenda
Gojo, I.; Tidwell, M.L.; Greer, J.; Takebe, N.; Seiter, K.; Pochron, M.F.; Johnson, B.; Sznol, M.; Karp, J.E.
Phase I and pharmacokinetic study of triapine, a potent ribonucleotide reductase inhibitor, in adults with advanced hematologic malignancies
Leuk. Res.
31
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2007
Homo sapiens
brenda
Karp, J.E.; Giles, F.J.; Gojo, I.; Morris, L.; Greer, J.; Johnson, B.; Thein, M.; Sznol, M.; Low, J.
A phase I study of the novel ribonucleotide reductase inhibitor 3-aminopyridine-2-carboxaldehyde thiosemicarbazone (3-AP, Triapine) in combination with the nucleoside analog fludarabine for patients with refractory acute leukemias and aggressive myeloprol
Leuk. Res.
32
71-77
2008
Homo sapiens
brenda
Saiko, P.; Pemberger, M.; Horvath, Z.; Savinc, I.; Grusch, M.; Handler, N.; Erker, T.; Jaeger, W.; Fritzer-Szekeres, M.; Szekeres, T.
Novel resveratrol analogs induce apoptosis and cause cell cycle arrest in HT29 human colon cancer cells: inhibition of ribonucleotide reductase activity
Oncol. Rep.
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2008
Homo sapiens
brenda
Lohman, G.J.; Gerfen, G.J.; Stubbe, J.
Inactivation of Lactobacillus leichmannii ribonucleotide reductase by 2,2-difluoro-2-deoxycytidine 5-triphosphate: adenosylcobalamin destruction and formation of a nucleotide-based radical
Biochemistry
49
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2010
Lactobacillus leichmannii
brenda
Lohman, G.J.; Stubbe, J.
Inactivation of Lactobacillus leichmannii ribonucleotide reductase by 2',2'-difluoro-2'-deoxycytidine 5'-triphosphate: covalent modification
Biochemistry
49
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Lactobacillus leichmannii
brenda
Holmgren, A.; Sengupta, R.
The use of thiols by ribonucleotide reductase
Free Radic. Biol. Med.
49
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Tequatrovirus T4, Escherichia coli, Mus musculus
brenda
Pontarin, G.; Ferraro, P.; Rampazzo, C.; Kollberg, G.; Holme, E.; Reichard, P.; Bianchi, V.
Deoxyribonucleotide metabolism in cycling and resting human fibroblasts with a missense mutation in p53R2, a subunit of ribonucleotide reductase
J. Biol. Chem.
286
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2011
Homo sapiens
brenda
Logan, D.
Closing the circle on ribonucleotide reductases
Nat. Struct. Mol. Biol.
18
251-253
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Escherichia coli, Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Ylikallio, E.; Page, J.L.; Xu, X.; Lampinen, M.; Bepler, G.; Ide, T.; Tyynismaa, H.; Weiss, R.S.; Suomalainen, A.
Ribonucleotide reductase is not limiting for mitochondrial DNA copy number in mice
Nucleic Acids Res.
38
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2010
Mus musculus
brenda
Halimi, Y.; Dessau, M.; Pollak, S.; Ast, T.; Erez, T.; Livnat-Levanon, N.; Karniol, B.; Hirsch, J.; Chamovitz, D.
COP9 signalosome subunit 7 from Arabidopsis interacts with and regulates the small subunit of ribonucleotide reductase (RNR2)
Plant Mol. Biol.
77
77-89
2011
Arabidopsis thaliana (P50651), Arabidopsis thaliana (Q9LSD0), Arabidopsis thaliana Col-0 (P50651), Arabidopsis thaliana Col-0 (Q9LSD0)
brenda
Panosa, A.; Roca, I.; Gibert, I.
Ribonucleotide reductases of Salmonella typhimurium: transcriptional regulation and differential role in pathogenesis
PLoS ONE
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e11328
2010
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Manzerova, J.; Krymov, V.; Gerfen, G.J.
Investigating the intermediates in the reaction of ribonucleoside triphosphate reductase from Lactobacillus leichmannii: An application of HF EPR-RFQ technology
J. Magn. Reson.
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32-45
2011
Lactobacillus leichmannii (Q59490), Lactobacillus leichmannii
brenda
Alnajar, S.; Khadka, B.; Gupta, R.
Ribonucleotide reductases from bifidobacteria contain multiple conserved indels distinguishing them from all other organisms In silico analysis of the possible role of a 43 aa bifidobacteria-specific insert in the class III RNR homolog
Front. Microbiol.
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1409
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Bifidobacterium longum
brenda
Aurelius, O.; Johansson, R.; Bagenholm, V.; Lundin, D.; Tholander, F.; Balhuizen, A.; Beck, T.; Sahlin, M.; Sjoeberg, B.M.; Mulliez, E.; Logan, D.T.
The crystal structure of Thermotoga maritima class III ribonucleotide reductase lacks a radical cysteine pre-positioned in the active site
PLoS ONE
10
e0128199
2015
Thermotoga maritima (Q9WYL6), Thermotoga maritima
brenda
Arnaoutov, A.; Dasso, M.
Enzyme regulation. IRBIT is a novel regulator of ribonucleotide reductase in higher eukaryotes
Science
345
1512-1515
2014
Homo sapiens
brenda
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