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Information on EC 1.17.4.2 - ribonucleoside-triphosphate reductase (thioredoxin) and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LSD0
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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 taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected 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, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2'-deoxyribonucleoside-triphosphate:oxidized-thioredoxin 2'-oxidoreductase
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-
-
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ribonucleoside triphosphate reductase
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-
-
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ribonucleotide reductase
ribonucleotide reductase
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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).
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
additional information
?
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the small subunit of RNR2 interacts in planta with the C-terminal section of signalosome protein complex COP9 subunit 7, CSN7, overview
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-
?
additional information
?
-
the small subunit of RNR2 interacts in planta with the C-terminal section of signalosome protein complex COP9 subunit 7, CSN7, overview
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-
?
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
-
-
?
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
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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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
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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
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
additional information
-
expression of subunit isoform RNR2B in all tissues tested, but at low level
additional information
expression of subunit isoform RNR2B in all tissues tested, but at low level
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
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
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
the subcellular localization of RNR2 is primarily nuclear in meristematic regions, and cytoplasmic in adult cells. RNR2 is constitutively nuclear in csn7 mutant seedlings
the subcellular localization of RNR2 is primarily nuclear in meristematic regions, and cytoplasmic in adult cells. RNR2 is constitutively nuclear in csn7 mutant seedlings
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant RNR2 from transgenic Arabidopsis thaliana plants by affinity chromatography
recombinant RNR2 from transgenic Arabidopsis thaliana plants by affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
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
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)
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