BRENDA - Enzyme Database
show all sequences of 1.17.4.2

The use of thiols by ribonucleotide reductase

Holmgren, A.; Sengupta, R.; Free Radic. Biol. Med. 49, 1617-1628 (2010)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
caracemide
-
Escherichia coli
caracemide
-
Escherichia virus T4
caracemide
-
Mus musculus
chlorambucil
-
Escherichia coli
chlorambucil
-
Escherichia virus T4
chlorambucil
-
Mus musculus
cisplatin
-
Escherichia coli
cisplatin
-
Escherichia virus T4
cisplatin
-
Mus musculus
Co2+
RNR activity chelates with copper leading to inactivation
Escherichia coli
Co2+
RNR activity chelates with copper leading to inactivation
Escherichia virus T4
Co2+
RNR activity chelates with copper leading to inactivation
Mus musculus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
class II enzymes contain cobalamin as cofactor
Escherichia coli
Co2+
class II enzymes contain cobalamin as cofactor
Mus musculus
Fe2+
the class III enzymes contain 4Fe-4S clusters in the small beta-subunit
Escherichia coli
Fe2+
the class III enzymes contain 4Fe-4S clusters in the small beta-subunit
Escherichia virus T4
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
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
Mus musculus
class II RNRs convert nucleoside triphosphates and nucleoside 5'-diphosphates, see also EC 1.17.4.1, to the correspondent 2'deoxy products, overview
?
-
-
-
nucleoside 5'-triphosphate + formate
Escherichia coli
class III RNR
2'-deoxynucleoside 5'-triphosphate + H2O
-
-
?
nucleoside 5'-triphosphate + formate
Escherichia virus T4
class III RNR
2'-deoxynucleoside 5'-triphosphate + H2O
-
-
?
nucleoside 5'-triphosphate + thioredoxin
Mus musculus
class II RNRs
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
-
?
nucleoside 5'-triphosphate + thioredoxin
Escherichia coli
class II RNRs
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Escherichia virus T4
-
-
-
Mus musculus
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
715085
Escherichia coli
?
-
-
-
-
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
715085
Mus musculus
?
-
-
-
-
additional information
the class II RNR also uses nucleoside 5'-diphosphate as substrate
715085
Mus musculus
?
-
-
-
-
additional information
the class II RNR also uses nucleoside 5'-diphosphate as substrate
715085
Escherichia coli
?
-
-
-
-
nucleoside 5'-triphosphate + formate
class III RNR
715085
Escherichia coli
2'-deoxynucleoside 5'-triphosphate + H2O
-
-
-
?
nucleoside 5'-triphosphate + formate
class III RNR
715085
Escherichia virus T4
2'-deoxynucleoside 5'-triphosphate + H2O
-
-
-
?
nucleoside 5'-triphosphate + thioredoxin
class II RNRs
715085
Mus musculus
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
-
-
?
nucleoside 5'-triphosphate + thioredoxin
class II RNRs
715085
Escherichia coli
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer or dimer
alpha or alpha2, class II RNRs
Escherichia coli
monomer or dimer
alpha or alpha2, class II RNRs
Mus musculus
More
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
Escherichia coli
More
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
Escherichia virus T4
More
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
Mus musculus
tetramer
alpha2beta2, class III RNRs
Escherichia coli
tetramer
alpha2beta2, class III RNRs
Escherichia virus T4
Cofactor
Cofactor
Commentary
Organism
Structure
5'-deoxyadenosylcobalamin
class II enzymes
Escherichia coli
5'-deoxyadenosylcobalamin
class II enzymes
Mus musculus
Cobalamin
class II enzymes
Escherichia coli
Cobalamin
class II enzymes
Mus musculus
additional information
cofactor specificity and binding, role in reaction, overview; the class III enzymes contain 4Fe-4S clusters in the small beta-subunit. Cofactor specificity and binding, role in reaction, overview
Escherichia coli
additional information
the class III enzymes contain 4Fe-4S clusters in the small beta-subunit. Cofactor specificity and binding, role in reaction, overview
Escherichia virus T4
additional information
cofactor specificity and binding, role in reaction, overview
Mus musculus
S-adenosyl-L-methionine
-
Escherichia coli
S-adenosyl-L-methionine
-
Escherichia virus T4
thioredoxin
-
Escherichia coli
thioredoxin
class II enzymes
Mus musculus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
5'-deoxyadenosylcobalamin
class II enzymes
Escherichia coli
5'-deoxyadenosylcobalamin
class II enzymes
Mus musculus
Cobalamin
class II enzymes
Escherichia coli
Cobalamin
class II enzymes
Mus musculus
additional information
cofactor specificity and binding, role in reaction, overview; the class III enzymes contain 4Fe-4S clusters in the small beta-subunit. Cofactor specificity and binding, role in reaction, overview
Escherichia coli
additional information
the class III enzymes contain 4Fe-4S clusters in the small beta-subunit. Cofactor specificity and binding, role in reaction, overview
Escherichia virus T4
additional information
cofactor specificity and binding, role in reaction, overview
Mus musculus
S-adenosyl-L-methionine
-
Escherichia coli
S-adenosyl-L-methionine
-
Escherichia virus T4
thioredoxin
-
Escherichia coli
thioredoxin
class II enzymes
Mus musculus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
caracemide
-
Escherichia coli
caracemide
-
Escherichia virus T4
caracemide
-
Mus musculus
chlorambucil
-
Escherichia coli
chlorambucil
-
Escherichia virus T4
chlorambucil
-
Mus musculus
cisplatin
-
Escherichia coli
cisplatin
-
Escherichia virus T4
cisplatin
-
Mus musculus
Co2+
RNR activity chelates with copper leading to inactivation
Escherichia coli
Co2+
RNR activity chelates with copper leading to inactivation
Escherichia virus T4
Co2+
RNR activity chelates with copper leading to inactivation
Mus musculus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
class II enzymes contain cobalamin as cofactor
Escherichia coli
Co2+
class II enzymes contain cobalamin as cofactor
Mus musculus
Fe2+
the class III enzymes contain 4Fe-4S clusters in the small beta-subunit
Escherichia coli
Fe2+
the class III enzymes contain 4Fe-4S clusters in the small beta-subunit
Escherichia virus T4
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Escherichia coli
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
Mus musculus
class II RNRs convert nucleoside triphosphates and nucleoside 5'-diphosphates, see also EC 1.17.4.1, to the correspondent 2'deoxy products, overview
?
-
-
-
nucleoside 5'-triphosphate + formate
Escherichia coli
class III RNR
2'-deoxynucleoside 5'-triphosphate + H2O
-
-
?
nucleoside 5'-triphosphate + formate
Escherichia virus T4
class III RNR
2'-deoxynucleoside 5'-triphosphate + H2O
-
-
?
nucleoside 5'-triphosphate + thioredoxin
Mus musculus
class II RNRs
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
-
?
nucleoside 5'-triphosphate + thioredoxin
Escherichia coli
class II RNRs
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
715085
Escherichia coli
?
-
-
-
-
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
715085
Mus musculus
?
-
-
-
-
additional information
the class II RNR also uses nucleoside 5'-diphosphate as substrate
715085
Mus musculus
?
-
-
-
-
additional information
the class II RNR also uses nucleoside 5'-diphosphate as substrate
715085
Escherichia coli
?
-
-
-
-
nucleoside 5'-triphosphate + formate
class III RNR
715085
Escherichia coli
2'-deoxynucleoside 5'-triphosphate + H2O
-
-
-
?
nucleoside 5'-triphosphate + formate
class III RNR
715085
Escherichia virus T4
2'-deoxynucleoside 5'-triphosphate + H2O
-
-
-
?
nucleoside 5'-triphosphate + thioredoxin
class II RNRs
715085
Mus musculus
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
-
-
?
nucleoside 5'-triphosphate + thioredoxin
class II RNRs
715085
Escherichia coli
2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer or dimer
alpha or alpha2, class II RNRs
Escherichia coli
monomer or dimer
alpha or alpha2, class II RNRs
Mus musculus
More
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
Escherichia coli
More
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
Escherichia virus T4
More
structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview
Mus musculus
tetramer
alpha2beta2, class III RNRs
Escherichia coli
tetramer
alpha2beta2, class III RNRs
Escherichia virus T4
General Information
General Information
Commentary
Organism
additional information
the class III RNR reaction involves deoxyadenosyl, glycyl, or cysteinyl radicals and requires anaerobic conditions; 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
Escherichia coli
additional information
Cys290 in class III from bacteriophage T4 are the conserved cysteine residues that are the sites for generation of the thiyl radical
Escherichia virus T4
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
Mus musculus
physiological function
during anaerobic growth, Escherichia coli depends on a class III RNR for the synthesis of deoxyribonucleotides
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
additional information
the class III RNR reaction involves deoxyadenosyl, glycyl, or cysteinyl radicals and requires anaerobic conditions; 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
Escherichia coli
additional information
Cys290 in class III from bacteriophage T4 are the conserved cysteine residues that are the sites for generation of the thiyl radical
Escherichia virus T4
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
Mus musculus
physiological function
during anaerobic growth, Escherichia coli depends on a class III RNR for the synthesis of deoxyribonucleotides
Escherichia coli
Other publictions for EC 1.17.4.2
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
744978
Alnajar
Ribonucleotide reductases fro ...
Bifidobacterium longum
Front. Microbiol.
8
1409
2017
-
-
-
-
-
-
-
-
-
-
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4
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1
1
-
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-
746184
Aurelius
The crystal structure of Ther ...
Thermotoga maritima
PLoS ONE
10
e0128199
2015
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-
-
1
-
-
-
-
-
-
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-
8
-
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1
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1
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1
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746494
Arnaoutov
Enzyme regulation. IRBIT is a ...
Homo sapiens
Science
345
1512-1515
2014
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-
-
-
-
-
1
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-
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3
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1
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1
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1
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-
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-
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-
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-
715583
Pontarin
Deoxyribonucleotide metabolism ...
Homo sapiens
J. Biol. Chem.
286
11132-11140
2011
-
-
1
-
1
-
-
-
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2
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2
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1
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1
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1
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2
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1
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-
2
2
-
-
-
716317
Logan
Closing the circle on ribonucl ...
Escherichia coli, Pseudomonas aeruginosa, Salmonella enterica subsp. enterica serovar Typhimurium
Nat. Struct. Mol. Biol.
18
251-253
2011
-
-
-
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-
-
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-
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3
-
3
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6
4
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3
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6
4
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3
3
-
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716563
Halimi
COP9 signalosome subunit 7 fro ...
Arabidopsis thaliana, Arabidopsis thaliana Col-0
Plant Mol. Biol.
77
77-89
2011
-
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1
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1
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1
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3
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4
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6
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1
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2
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4
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2
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1
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2
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5
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4
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2
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4
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4
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1
1
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728091
Manzerova
Investigating the intermediate ...
Lactobacillus leichmannii
J. Magn. Reson.
213
32-45
2011
-
1
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4
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714185
Lohman
Inactivation of Lactobacillus ...
Lactobacillus leichmannii
Biochemistry
49
1396-1403
2010
-
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1
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1
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1
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2
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2
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1
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1
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1
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1
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1
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1
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1
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2
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1
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1
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714186
Lohman
Inactivation of Lactobacillus ...
Lactobacillus leichmannii
Biochemistry
49
1404-1417
2010
-
-
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-
1
-
2
-
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-
1
1
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2
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2
1
1
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1
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1
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1
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1
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2
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1
1
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2
1
1
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1
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715085
Holmgren
The use of thiols by ribonucle ...
Escherichia coli, Escherichia virus T4, Mus musculus
Free Radic. Biol. Med.
49
1617-1628
2010
-
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-
12
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4
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6
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3
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8
7
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11
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11
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12
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4
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6
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8
7
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4
4
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-
716377
Ylikallio
Ribonucleotide reductase is no ...
Mus musculus
Nucleic Acids Res.
38
8208-8218
2010
-
-
1
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1
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1
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4
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1
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1
3
3
1
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716674
Panosa
Ribonucleotide reductases of S ...
Salmonella enterica subsp. enterica serovar Typhimurium
PLoS ONE
5
e11328
2010
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1
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2
2
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687196
Roca
Fumarate and nitrate reduction ...
Escherichia coli K-12
Int. Microbiol.
11
49-56
2008
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687199
Odenike
Phase I study of the ribonucle ...
Homo sapiens
Invest. New Drugs
26
233-239
2008
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688754
Karp
A phase I study of the novel r ...
Homo sapiens
Leuk. Res.
32
71-77
2008
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1
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689295
Saiko
Novel resveratrol analogs indu ...
Homo sapiens
Oncol. Rep.
19
1621-1626
2008
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1
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671925
Lin
Excess ribonucleotide reductas ...
Homo sapiens
Biochem. Pharmacol.
73
760-772
2007
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672890
Madlener
Gallic acid inhibits ribonucle ...
Homo sapiens
Cancer Lett.
245
156-162
2007
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2
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673802
Camier
Visualization of ribonucleotid ...
Saccharomyces cerevisiae
Free Radic. Biol. Med.
42
1008-1016
2007
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1
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676528
Garton
crinkled leaves 8 - A mutation ...
Arabidopsis thaliana
Plant J.
50
118-127
2007
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1
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685023
Sigmond
The synergistic interaction of ...
Homo sapiens
Biochem. Pharmacol.
73
1548-1557
2007
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3
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686091
Cerqueira
Understanding ribonucleotide r ...
Escherichia coli
Chemistry
13
8507-8515
2007
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687180
Saiko
N-hydroxy-N-(3,4,5-trimethoxyp ...
Homo sapiens
Int. J. Oncol.
31
1261-1266
2007
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688750
Gojo
Phase I and pharmacokinetic st ...
Homo sapiens
Leuk. Res.
31
1165-1173
2007
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1
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1
1
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673834
Pham
Regulation of the ribonucleoti ...
Aedes aegypti
Gene
372
182-190
2006
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1
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674765
Hakansson
Regulation of mammalian ribonu ...
Mus musculus
J. Biol. Chem.
281
7834-7841
2006
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676426
Wang
Arabidopsis ribonucleotide red ...
Arabidopsis thaliana
Plant Cell
18
350-365
2006
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1
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7
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7
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659464
Torrents
Two proteins mediate class II ...
Pseudomonas aeruginosa
J. Biol. Chem.
280
16571-16578
2005
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3
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1
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2
1
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671912
Liu
The ribonucleotide reductase s ...
Homo sapiens
Biochem. Pharmacol.
70
1288-1297
2005
-
-
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2
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2
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1
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1
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-
659994
Larsson
Structural mechanism of allost ...
Thermotoga maritima
Nat. Struct. Mol. Biol.
11
1142-1149
2004
-
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1
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2
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-
-
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-
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-
657991
Chen
Epimerization at carbon-5' of ...
Lactobacillus leichmannii
Biochemistry
42
4578-4584
2003
1
-
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2
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2
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2
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1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
660352
Logan
A metal-binding site in the ca ...
Escherichia coli, Escherichia coli JM109
Proc. Natl. Acad. Sci. USA
100
3826-3831
2003
-
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-
1
4
-
-
-
-
-
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33
-
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1
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-
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2
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1
4
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1
-
-
-
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2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437906
Hoegbom
Crystal structure of the di-ir ...
Corynebacterium ammoniagenes
Biochemistry
41
1381-1389
2002
-
-
-
-
-
-
-
-
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1
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4
-
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6
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1
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-
-
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6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437904
Chabes
Yeast ribonucleotide reductase ...
Saccharomyces cerevisiae
Proc. Natl. Acad. Sci. USA
97
2474-2479
2000
-
-
-
-
-
-
-
-
-
-
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1
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3
-
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1
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-
-
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2
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1
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1
-
-
-
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2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437899
Jordan
Ribonucleotide reduction in Ps ...
Brevundimonas diminuta, Brevundimonas vesicularis, Burkholderia cepacia, Deinococcus radiodurans, Delftia acidovorans, Escherichia coli, Hydrogenophaga flava, Lactobacillus leichmannii, Mycobacterium tuberculosis, Paracoccus denitrificans, Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas sp., Pseudomonas stutzeri, Ralstonia pickettii, Stenotrophomonas maltophilia, Xanthomonas campestris
J. Bacteriol.
181
3974-3980
1999
-
-
-
-
-
-
-
-
-
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-
17
-
17
-
-
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-
-
-
-
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34
-
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4
-
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-
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4
-
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17
-
-
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-
-
-
-
-
34
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437900
Licht
Studies on the catalysis of ca ...
Escherichia coli, Lactobacillus leichmannii
Biochemistry
38
1221-1233
1999
-
-
-
-
-
-
-
2
-
-
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2
-
3
-
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5
-
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1
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1
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2
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2
-
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-
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-
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5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437901
Licht
Thermodynamic and kinetic stud ...
Lactobacillus leichmannii
Biochemistry
38
1234-1242
1999
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
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2
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-
-
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-
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1
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-
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-
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1
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-
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-
-
-
-
-
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1
-
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-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437902
Suto
-
Ribonucleoside triphosphate re ...
Lactobacillus leichmannii
Bioorg. Chem.
27
451-462
1999
1
-
1
-
-
-
8
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
8
-
-
1
-
1
1
-
-
-
-
8
8
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437903
Suto
Adenosylcobalamin-dependent ri ...
Lactobacillus leichmannii
Prep. Biochem. Biotechnol.
29
273-309
1999
1
-
1
1
-
-
-
-
-
-
2
1
-
2
-
-
1
-
-
-
-
-
4
-
-
-
-
6
-
-
-
1
-
-
-
1
-
1
1
1
-
-
-
-
-
-
-
-
2
1
-
-
-
1
-
-
-
-
4
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
437897
Jordan
B12-dependent ribonucleotide r ...
Archaeoglobus fulgidus, Chloroflexus aurantiacus, Deinococcus radiodurans, Deinococcus radiodurans R1 / ATCC 13939 / DSM 20539, Escherichia coli, Lactobacillus leichmannii, Methanocaldococcus jannaschii, Mycobacterium tuberculosis, Pyrococcus furiosus, Thermoplasma acidophilum, Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Proc. Natl. Acad. Sci. USA
94
13487-13492
1997
5
-
2
-
-
-
5
-
-
5
3
12
-
48
-
-
2
-
-
-
-
-
36
-
1
-
-
-
-
-
-
4
-
-
-
5
-
2
4
-
-
-
-
5
-
-
-
5
3
12
-
-
-
2
-
-
-
-
36
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
437898
Tauer
The B12-dependent ribonucleoti ...
Anabaena sp., Escherichia coli, Halobacterium salinarum, Haloferax volcanii, Homo sapiens, Lactobacillus leichmannii, Mycobacterium tuberculosis, Thermoplasma acidophilum, Thermus aquaticus, Thermus aquaticus X1
Proc. Natl. Acad. Sci. USA
94
53-58
1997
2
-
1
-
-
-
-
-
-
-
1
10
-
19
-
-
1
-
-
-
1
-
20
-
1
-
-
-
-
-
-
3
-
-
-
2
-
1
3
-
-
-
-
-
-
-
-
-
1
10
-
-
-
1
-
-
1
-
20
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
437896
Booker
Coenzyme B12-dependent ribonuc ...
Lactobacillus leichmannii
Biochemistry
33
12676-12685
1994
-
-
1
-
-
-
-
-
-
-
1
1
-
3
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
1
-
-
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-
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1
1
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-
-
-
-
-
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1
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437895
Halicky
Immobilization of ribonucleoti ...
Kitasatospora aureofaciens
Collect. Czech. Chem. Commun.
54
2528-2541
1989
2
-
-
-
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1
-
8
-
2
-
1
-
2
-
-
-
-
-
2
-
-
8
1
1
-
-
-
1
1
-
1
-
-
-
2
-
-
1
-
-
1
-
-
-
8
-
2
-
1
-
-
-
-
-
2
-
-
8
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
437894
Ashley
The mechanism of Lactobacillus ...
Lactobacillus leichmannii
J. Biol. Chem.
261
3958-3964
1986
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437893
Gleason
Adenosylcobalamin-dependent ri ...
Anabaena sp., Anabaena sp. 7119, Escherichia coli, Lactobacillus leichmannii
J. Biol. Chem.
255
7728-7733
1980
6
-
-
-
-
-
2
1
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2
4
3
-
13
-
-
1
-
-
1
1
-
28
3
-
-
-
-
1
-
-
1
-
-
-
6
-
-
1
-
-
-
-
2
-
1
-
2
4
3
-
-
-
1
-
1
1
-
28
3
-
-
-
-
1
-
-
-
-
-
-
-
-
-
437892
Blakley
Ribonucleoside triphosphate re ...
Astasia sp., Clostridium sp., Corynebacterium sp., Euglena sp., Lactobacillus leichmannii, Pseudomonas sp., Rhizobium sp.
Methods Enzymol.
51
246-259
1978
4
-
-
-
-
1
6
5
-
6
1
7
-
8
-
-
1
-
-
-
1
1
25
1
-
-
-
-
-
-
-
9
-
-
-
4
-
-
9
-
-
1
-
6
-
5
-
6
1
7
-
-
-
1
-
-
1
1
25
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437890
Chen
Substrate and effector binding ...
Lactobacillus leichmannii
Biochemistry
13
654-661
1974
4
-
-
-
-
-
-
-
-
-
7
2
-
2
-
-
1
-
-
-
1
1
3
1
-
-
-
-
-
-
-
1
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
7
2
-
-
-
1
-
-
1
1
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437891
Hamilton
Ribonucleotide reductase from ...
Escherichia coli, Euglena gracilis, Euglena gracilis Z, Lactobacillus leichmannii
J. Biol. Chem.
249
4428-4434
1974
11
-
-
-
-
-
2
4
-
2
4
3
-
24
-
-
3
-
-
-
1
-
23
1
-
-
-
-
-
-
-
1
-
-
-
11
-
-
1
-
-
-
-
2
-
4
-
2
4
3
-
-
-
3
-
-
1
-
23
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437889
Sando
Ribonucleotide reductase from ...
Lactobacillus leichmannii, Thermus aquaticus, Thermus aquaticus YT-1, Thermus sp., Thermus sp. X-1
Biochemistry
12
3316-3322
1973
1
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-
-
-
-
-
5
-
2
1
4
-
25
-
-
2
-
-
-
-
1
35
1
2
2
-
-
1
-
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
5
-
2
1
4
-
-
-
2
-
-
-
1
35
1
2
2
-
-
1
-
-
-
-
-
-
-
-
-
681889
Yau
The Bacillus megaterium ribonu ...
Bacillus megaterium, Bacillus megaterium KM / ATCC 13632
Mol. Cell. Biochem.
1
101-105
1973
1
-
-
-
-
-
1
-
-
1
-
-
-
12
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
1
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437888
Goulian
Purification and properties of ...
Lactobacillus leichmannii
J. Biol. Chem.
241
4233-4242
1966
3
-
-
-
-
-
2
3
-
-
1
1
-
2
-
-
1
-
-
-
1
3
11
-
-
-
-
-
-
-
-
3
-
-
-
3
-
-
3
-
-
-
-
2
-
3
-
-
1
1
-
-
-
1
-
-
1
3
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
437887
Bakley
Cobamides and ribonucleotide r ...
Lactobacillus leichmannii
J. Biol. Chem.
240
2173-2180
1965
15
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
15
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
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-