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Information on EC 1.17.4.1 - ribonucleoside-diphosphate reductase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P21524
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1.17.4.1 ribonucleoside-diphosphate reductaseIUBMB Comments
This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. There are three types of this enzyme differing in their cofactors. Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which 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) and EC 1.17.4.2, ribonucleoside-triphosphate reductase (thioredoxin).
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Word Map
- 1.17.4.1
- deoxyribonucleotides
- hydroxyurea
-
tyrosyl
- reductases
- chlamydia
- trachomatis
-
deoxynucleotides
-
proton-coupled
-
diiron
- deoxycytidine
-
diferric
-
thiyl
- dntps
- dcdp
- thiosemicarbazone
-
diferric-tyrosyl
-
nrdabs
-
hydroxyurea-resistant
- medicine
-
nrdef
-
heterodinuclear
- drug development
-
antiferromagnetically
- pharmacology
- molecular biology
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
ribonucleoside diphosphate reductase, cdp reductase, class i rnr, class i ribonucleotide reductase, class ia rnr, ribonucleoside-diphosphate reductase, class ia ribonucleotide reductase, adp reductase, p53-inducible ribonucleotide reductase, class ic ribonucleotide reductase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2'-deoxyribonucleoside-diphosphate:oxidized-thioredoxin 2'-oxidoreductase
-
-
-
-
ADP reductase
-
-
-
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CDP reductase
-
-
-
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nucleoside diphosphate reductase
-
-
-
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reductase, ribonucleoside diphosphate
-
-
-
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ribonucleoside 5'-diphosphate reductase
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-
-
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ribonucleoside diphosphate reductase
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-
-
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ribonucleotide diphosphate reductase
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-
-
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ribonucleotide reductase
-
-
-
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UDP reductase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin
binding of specificity effector rearranges loop 2 and moves residue P294 out of the catalytic site, accomodating substrate binding. substrate binding further rearranges loop2. Cross-talk occurs largely through R293 and Q288 of loop 2. Substrate ribose binds with its 3 hydroxyl closer than its 2 hydroxyl to residue C218 of the catalytic redox pair
2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin
proposed mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
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oxidation
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-
-
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
2'-deoxyribonucleoside-5'-diphosphate:thioredoxin-disulfide 2'-oxidoreductase
This enzyme is responsible for the de novo conversion of ribonucleoside diphosphates into deoxyribonucleoside diphosphates, which are essential for DNA synthesis and repair. There are three types of this enzyme differing in their cofactors. Class Ia enzymes contain a diiron(III)-tyrosyl radical, class Ib enzymes contain a dimanganese-tyrosyl radical, and class II enzymes contain adenosylcobalamin. In all cases the cofactors are involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which 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) and EC 1.17.4.2, ribonucleoside-triphosphate reductase (thioredoxin).
CAS REGISTRY NUMBER
COMMENTARY
9047-64-7
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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
ADP + dithiothreitol
2'-dADP + oxidized dithiothreitol + H2O
-
-
-
?
CDP + dithiothreitol
2'-dCDP + oxidized dithiothreitol + H2O
-
-
-
?
GDP + thioredoxin
2'-deoxyGDP + thioredoxin disulfide + H2O
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-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
-
-
-
?
CDP + thioredoxin
2'-dCDP + thioredoxin disulfide + H2O
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CDP is the favored substrate. However, the kcat/Km values for ADP, GDP, and UDP are within 100-fold of the value for CDP
-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
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class Ia RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
class Ia RNRs
-
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
-
-
ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
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maximal activity with E. coli thioredoxin
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ir
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
additional information
?
-
-
DNA damage checkpoints modulate RNR activity through the temporal and spatial regulation of its subunits
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-
?
additional information
?
-
-
under normal conditions, the cell assembles stoichiometric amounts of tyrosyl radicals essential for enzyme activity per betabeta subunit dimer. Modulation of tyrosyl radical concentration is not involved in regulation of enzyme activity
-
-
?
additional information
?
-
-
class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor
-
-
?
additional information
?
-
-
C-terminus of one monomeric R1 subunit acts in trans to regenerate the active site of its neighboring monomer. The class I RNR active-site disulfide bridge between Cys225 and Cys462 must be reduced for a complete turnover. The electron required for this reduction is provided by a redox network, which involves a cysteine pair at the C-terminus of the R1 subunit, the thioredoxin or glutaredoxin system, and NADPH. For in vitro experiments, the disulfide bridge can be reduced by small thiol compounds such as DTT
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-
?
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
GDP + thioredoxin
2'-deoxyGDP + thioredoxin disulfide + H2O
-
-
-
?
ribonucleoside diphosphate + thioredoxin
2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O
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-
-
?
nucleoside 5'-diphosphate + glutaredoxin
2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
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class Ia RNRs
-
-
?
nucleoside 5'-diphosphate + thioredoxin
2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
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class Ia RNRs
-
-
?
ribonucleoside diphosphate + reduced thioredoxin
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
enzyme catalyzes the first unique step in DNA synthesis
-
?
additional information
?
-
-
DNA damage checkpoints modulate RNR activity through the temporal and spatial regulation of its subunits
-
-
?
additional information
?
-
-
class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
cofactor specificity and binding, role in reaction, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe3+
-
class I enzymes contain diferric(III)-tyrosyl radical cofactor
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
mammalian R2 C-terminal heptapeptide P7
Ac-1FTLDADF7, the inhibitor binds at bind at a contiguous site containing residues that are highly conserved among eukaryotes, binding structure, overview
peptide P6
1Fmoc(Me)PhgLDChaDF7, the inhibitor binds at a contiguous site containing residues that are highly conserved among eukaryotes. The Fmoc group in P6 peptide forms several hydrophobic interactions that contribute to its enhanced potency in binding to ScR1, binding structure, overview
Sml1
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inhibitor protein Sml1 competes with the C-terminal domain of subunit R1 for association with its N-terminal domain to hinder the accessibility of the CX2C motif to the active site for R1 regeneration during the catalytic cycle
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additional information
-
overview: naturally occuring inhibitors e.g. proteins and nucleotides
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additional information
-
not inhibited by 8-hydroxyquinoline and o-phenanthroline
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dATP
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binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop.. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
ATP
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binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. The unprotonated N1 of adenosine is the primary determinant of ATP/dATP-directed specificity for CDP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
dGTP
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binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. The O6 and protonated N1 of dGTP direct specificity for ADP. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
dTTP
-
binding of deoxynucleoside triphosphate effectors ATP/dATP, dGTP, and dTTP modulates the specificity of class I ribonucleotide reductase for CDP, UDP, ADP, and GDP substrates. dNTP effectors and NDP substrates bind on either side of a flexible nine-amino acid loop. Interactions with the effector nucleobase alter loop 2 geometry, resulting in changes in specificity among the four NDP substrates of ribonucleotide reductase
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.3
-
His-tagged subunit Y2-K387N, expressed in Saccharomyces cerevisiae
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
during the normal cell cycle, the two large subunits Rnr1 and Rnr3 are predominantly localized to cytoplasm. Under genotoxic stress the subunits Rnr2 and Rnr4 become redistributed to the cytoplasm in a checkpoint-dependent manner
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during the normal cell cycle, the two small subunits Rnr2 and Rnr4 are predominantly localized to nucleus. Under genotoxic stress, Rnr2 and Rnr4 become redistributed to the cytoplasm in a checkpoint-dependent manner
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme maintains balanced pools of deoxyribonucleotide substrates for DNA replication by converting ribonucleoside diphosphates to 2'-deoxyribonucleoside diphosphates
physiological function
-
the ribonucleotide reductase response to DNA damage does not operate similarly across the cell cycle at either the transcript or the protein level. Ribonucleotide reductase subunit mRNA levels are comparably low in both damaged and undamaged G1 cells and highly induced in damaged S/G2 cells. Transcript numbers becomes correlated with both protein levels and localization only upon DNA damage in a cell cycle-dependent manner. The differential ribonucleotide reductase response to DNA damage correlates with variable Mec1 kinase activity in the cell cycle in single cells. The transcription of ribonucleotide reductase genes is noisy and non-Poissonian in nature
additional information
-
the reaction of class Ia RNRs involves tyrosyl or cysteinyl radicals and requires aerobic conditions
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
tetramer
the enzyme activity requires formation of a complex between subunits R1 and R2 in which the R2 C-terminal peptide binds to R1
additional information
additional information
-
subunits Y1 and Y2 constitute the active enzyme, large subunit Y3 has no activity, subunit Y4 may function as a chaperone
additional information
-
C-terminal domain of subunit R1 acts in trans to reduce the active site of its neighbouring monomer and interacts with the N-terminal domain of neighbouring R1. Inhibitor protein Sml1 competes with the C-terminal domain of R1 for association with the N-terminal domain to hinder the accessibility of the CX2C motif to the active site for R1 regeneration during the catalytic cycle
additional information
-
enzyme consists of two homodimeric subunits, R1 and R2. In Saccharomyces cerevisiae, there are two R2 subunits named beta and beta, the active form in the holoenzyme being a dimer betabeta. Isoform beta plays a crucial role in cluster assembly
additional information
-
under normal conditions, the cell assembles stoichiometric amounts of tyrosyl radicals per betabeta subunit dimer and modulation of tyrosyl radical concentration is not involved in regulation of enzyme activity
additional information
-
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
alpha subunit, in apo form, in complex with AMP analogue 5'-adenylyl-beta,gamma-imidodiphosphate, with 5'-adenylyl-beta,gamma-imidodiphosphate and CDP, with 5'-adenylyl-beta,gamma-imidodiphosphate and UDP, with dGTP and ADP, TTP and GDP. Binding of specificity effector rearranges loop 2 and moves residue P294 out of the catalytic site, accomodating substrate binding. substrate binding further rearranges loop2. Cross-talk occurs largely through R293 and Q288 of loop 2. Substrate ribose binds with its 3 hydroxyl closer than its 2 hydroxyl to residue C218 of the catalytic redox pair
purified enzyme, formed by recombinant subunits R2 and R4, complexed with inhibitor peptide P7 or peptide Fmoc-P6, 20 mg/ml protein in 0.1 M HEPES, pH 7.5, with 20 mM TTP, 5% glycerol, 5mM DTT, 0.1 M KCL, and 25 mm MgCl2, is mixed with a reservoir solution containing 20-25% PEG 3350, 0.2 M NaCl, and 100 mM HEPES, pH 7.5, soaking of crystals for 4 h in reservoir solution with added inhibitor peptide P6 or P7, followed by soaking of crystals in 25% PEG 3350, 0.2 M NaCl, and 100 mM HEPES, pH 7.5, supplemented with 15% glycerol, X-ray diffraction structure determination and analysis at 2.6 and 2.5 A resolution, respectively
structures of mutanr R293A complexed with dGTP and AMPPNP-CDP reveal that ADP is not bound at the catalytic site, and CDP binds farther from the catalytic site compared to wild type
subunit Rnr1 in complex with gemcitabine diphosphate or with a beta subunit Rnr2 or Rnr4 derived peptide. Binding of gemcitabine diphosphate is different from binding of its analogue CDP. Rnr2 and Rnr4 peptides bind differently from each other and block the formation of the enzyme complex
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Q288A
mutation causes severe S phase defects in cells that use the enzyme as the sole source of of ribonucleoside diphosphate activity. Compared to the wild-type enzyme activity, Q288A mutants show 15% of ADP reduction, whereas they show 23% of CDP reduction. There is a 6fold loss of affinity for ADP binding and a 2fold loss of affinity for CDP. Q288A can support mitotic growth, albeit with a severe S phase defect
R293A
mutation causes lethality in cells that use the enzyme as the sole source of ribonucleoside diphosphate activity. Compared to the wild-type enzyme activity, R293A mutants show 4% of ADP reduction, whereas they show 20% CDP reduction. The mutant is unable to bind ADP and binds CDP with 2fold lower affinity compared to wild-type. X-ray structures of R293A complexed with dGTP and AMPPNP reveal that ADP is not bound at the catalytic site, and CDP binds farther from the catalytic site compared to wild type. R293A cannot support mitotic growth
C428S
-
mutantion is lethal. Cells carrying both the C428S and the SX2S mutation of CX2C motif on plasmids are viable and form colonies with an efficiency similar to that of the wild-type control showing interallelic complementation
K387N
-
affords higher activity due to increased tyrosyl radical content
additional information
additional information
construction of heterochimeric enzymes as heterocomplexes containing mammalian R2 C-terminal heptapeptide P7, Ac-1FTLDADF7, and its peptidomimetic P6, 1Fmoc(Me)PhgLDChaDF7, bound to Saccharomyces cerevisiae R1, ScR1, overview
additional information
-
construction of heterochimeric enzymes as heterocomplexes containing mammalian R2 C-terminal heptapeptide P7, Ac-1FTLDADF7, and its peptidomimetic P6, 1Fmoc(Me)PhgLDChaDF7, bound to Saccharomyces cerevisiae R1, ScR1, overview
additional information
-
deletion of C-terminal domain of subunit R1 is lethal. Mutation of CX2C motif to SX2S results in viable, but slowly growing cells. Mutant cells exhibit a prolonged S phase
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
partially purified enzyme is very unstable in solution, half-life at 0°C: less than 24 h
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
quick-freezing in liquid nitrogen and subsequent storage at -20°C, several weeks, no loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged subunits R2 and R4 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and dialysis
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged subunits R2 and R4 in Escherichia coli strain BL21(DE3)
expression of subunits Y1, Y2, Y3 and Y4 in Escherichia coli, expression of Y1, His-tagged Y2 and His tagged Y2-K387N mutant enzyme subunit in Saccharomyces cerevisiae
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ribonucleotide reductase subunit mRNA levels are comparably low in both damaged and undamaged G1 cells and highly induced in damaged S/G2 cells. Transcript numbers becomes correlated with both protein levels and localization only upon DNA damage in a cell cycle-dependent manner. The differential ribonucleotide reductase response to DNA damage correlates with variable Mec1 kinase activity in the cell cycle in single cells. The transcription of ribonucleotide reductase genes is noisy and non-Poissonian in nature
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lammers, M.; Follmann, H.
The ribonucleotide reductases - a unique group of metalloenzymes essential for cell proliferation
Struct. Bonding
54
27-91
1983
Tequatrovirus T4, Tequintavirus T5, Enterobacteria phage T6, Bos taurus, Saccharomyces cerevisiae, Oryctolagus cuniculus, Escherichia coli, Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus, Tetradesmus obliquus
-
Vitols, E.; Bauer, V.A.; Stanbrough, E.C.
Ribonucleotide reductase from Saccharomyces cerevisiae
Biochem. Biophys. Res. Commun.
41
71-77
1970
Saccharomyces cerevisiae, Herpes simplex virus
Nguyen, H.H.T.; Ge, J.; Perlstein, D.L.; Stubbe, J.
Purification of ribonucleotide reductase subunits Y1, Y2, Y3, and Y4 from yeast: Y4 plays a key role in diiron cluster assembly
Proc. Natl. Acad. Sci. USA
96
12339-12344
1999
Saccharomyces cerevisiae
Yao, R.; Zhang, Z.; An, X.; Bucci, B.; Perlstein, D.L.; Stubbe, J.; Huang, M.
Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways
Proc. Natl. Acad. Sci. USA
100
6628-6633
2003
Saccharomyces cerevisiae
Perlstein, D.L.; Ge, J.; Ortigosa, A.D.; Robblee, J.H.; Zhang, Z.; Huang, M.; Stubbe, J.
The active form of the Saccharomyces cerevisiae ribonucleotide reductase small subunit is a heterodimer in vitro and in vivo
Biochemistry
44
15366-15377
2005
Saccharomyces cerevisiae
Ortigosa, A.D.; Hristova, D.; Perlstein, D.L.; Zhang, Z.; Huang, M.; Stubbe, J.
Determination of the in vivo stoichiometry of tyrosyl radical per betabeta in Saccharomyces cerevisiae ribonucleotide reductase
Biochemistry
45
12282-12294
2006
Saccharomyces cerevisiae
Xu, H.; Faber, C.; Uchiki, T.; Fairman, J.W.; Racca, J.; Dealwis, C.
Structures of eukaryotic ribonucleotide reductase I provide insights into dNTP regulation
Proc. Natl. Acad. Sci. USA
103
4022-4027
2006
Saccharomyces cerevisiae (P21524)
Xu, H.; Faber, C.; Uchiki, T.; Racca, J.; Dealwis, C.
Structures of eukaryotic ribonucleotide reductase I define gemcitabine diphosphate binding and subunit assembly
Proc. Natl. Acad. Sci. USA
103
4028-4033
2006
Saccharomyces cerevisiae (P21524)
Zhang, Z.; Yang, K.; Chen, C.C.; Feser, J.; Huang, M.
Role of the C terminus of the ribonucleotide reductase large subunit in enzyme regeneration and its inhibition by Sml1
Proc. Natl. Acad. Sci. USA
104
2217-2222
2007
Saccharomyces cerevisiae, Escherichia coli
Xu, H.; Fairman, J.W.; Wijerathna, S.R.; Kreischer, N.R.; LaMacchia, J.; Helmbrecht, E.; Cooperman, B.S.; Dealwis, C.
The structural basis for peptidomimetic inhibition of eukaryotic ribonucleotide reductase: a conformationally flexible pharmacophore
J. Med. Chem.
51
4653-4659
2008
Saccharomyces cerevisiae (P21524), Saccharomyces cerevisiae
Holmgren, A.; Sengupta, R.
The use of thiols by ribonucleotide reductase
Free Radic. Biol. Med.
49
1617-1628
2010
Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Lactobacillus leichmannii, Mus musculus
Ahmad, M.F.; Kaushal, P.S.; Wan, Q.; Wijerathna, S.R.; An, X.; Huang, M.; Dealwis, C.G.
Role of arginine 293 and glutamine 288 in communication between catalytic and allosteric sites in yeast ribonucleotide reductase
J. Mol. Biol.
419
315-329
2012
Saccharomyces cerevisiae (P21524)
Mazumder, A.; Tummler, K.; Bathe, M.; Samson, L.D.
Single-cell analysis of ribonucleotide reductase transcriptional and translational response to DNA damage
Mol. Cell. Biol.
33
635-642
2013
Saccharomyces cerevisiae
Knappenberger, A.J.; Ahmad, M.F.; Viswanathan, R.; Dealwis, C.G.; Harris, M.E.
Nucleoside analogue triphosphates allosterically regulate human ribonucleotide reductase and identify chemical determinants that drive substrate specificity
Biochemistry
55
5884-5896
2016
Saccharomyces cerevisiae, Homo sapiens (P23921), Homo sapiens (P23921 and P31350), Homo sapiens
EXTERNAL LINKS (specific for EC-Number 1.17.4.1)
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