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Literature summary for 1.17.4.1 extracted from

  • Holmgren, A.; Sengupta, R.
    The use of thiols by ribonucleotide reductase (2010), Free Radic. Biol. Med., 49, 1617-1628.
    View publication on PubMed
Search for more literature for 1.17.4.1

Inhibitors

Inhibitors Comment Organism Structure
caracemide
-
 Escherichia coli
caracemide
-
 Homo sapiens
caracemide
-
 Lactobacillus leichmannii
caracemide
-
 Mus musculus
caracemide
-
 Saccharomyces cerevisiae
chlorambucil
-
 Escherichia coli
chlorambucil
-
 Homo sapiens
chlorambucil
-
 Lactobacillus leichmannii
chlorambucil
-
 Mus musculus
chlorambucil
-
 Saccharomyces cerevisiae
cisplatin
-
 Escherichia coli
cisplatin
-
 Homo sapiens
cisplatin
-
 Lactobacillus leichmannii
cisplatin
-
 Mus musculus
cisplatin
-
 Saccharomyces cerevisiae
Co2+ RNR activity chelates with copper leading to inactivation Escherichia coli
Co2+ RNR activity chelates with copper leading to inactivation Homo sapiens
Co2+ RNR activity chelates with copper leading to inactivation Lactobacillus leichmannii
Co2+ RNR activity chelates with copper leading to inactivation Mus musculus
Co2+ RNR activity chelates with copper leading to inactivation Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ class II enzymes contain cobalamin as cofactor Mus musculus
Co2+ class II enzymes contain cobalamin as cofactor Escherichia coli
Co2+ class II enzymes contain cobalamin as cofactor Lactobacillus leichmannii
Fe class I enzymes contain diferric(III)-tyrosyl radical cofactor Escherichia coli
Fe3+ class I enzymes contain diferric(III)-tyrosyl radical cofactor Mus musculus
Fe3+ class I enzymes contain diferric(III)-tyrosyl radical cofactor Homo sapiens
Fe3+ class I enzymes contain diferric(III)-tyrosyl radical cofactor Saccharomyces cerevisiae
Fe3+ class I enzymes contain diferric(III)-tyrosyl radical cofactor Lactobacillus leichmannii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview ?
-
 ?
additional information Escherichia coli class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview ?
-
 ?
additional information Lactobacillus leichmannii class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview ?
-
 ?
additional information Homo sapiens class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor ?
-
 ?
additional information Saccharomyces cerevisiae class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor ?
-
 ?
nucleoside 5'-diphosphate + glutaredoxin Mus musculus class I RNRs 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + glutaredoxin Escherichia coli class I RNRs 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + glutaredoxin Lactobacillus leichmannii class I RNRs 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + glutaredoxin Homo sapiens class Ia RNRs 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + glutaredoxin Saccharomyces cerevisiae class Ia RNRs 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + NrdH-redoxin Mus musculus only class Ib RNRs 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + NrdH-redoxin Escherichia coli only class Ib RNRs 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + NrdH-redoxin Lactobacillus leichmannii only class Ib RNRs 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + thioredoxin Mus musculus class I and class II RNRs 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + thioredoxin Escherichia coli class I and class II RNRs 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + thioredoxin Lactobacillus leichmannii class I and class II RNRs 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + thioredoxin Homo sapiens class Ia RNRs 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + thioredoxin Saccharomyces cerevisiae class Ia RNRs 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Homo sapiens
-
-
-
Lactobacillus leichmannii
-
-
-
Mus musculus
-
-
-
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview Mus musculus ?
-
 ?
additional information class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview Escherichia coli ?
-
 ?
additional information class Ia and Ib RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor. Class II RNRs catalyze the same reaction but also convert nucleoside triphosphates to the correspondent 2'deoxy products, EC 1.17.4.2, overview Lactobacillus leichmannii ?
-
 ?
additional information class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor Homo sapiens ?
-
 ?
additional information class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor Saccharomyces cerevisiae ?
-
 ?
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 Saccharomyces cerevisiae ?
-
 ?
additional information 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 Mus musculus ?
-
 ?
additional information 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 Escherichia coli ?
-
 ?
additional information 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 Homo sapiens ?
-
 ?
additional information 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 Lactobacillus leichmannii ?
-
 ?
nucleoside 5'-diphosphate + glutaredoxin class I RNRs Mus musculus 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + glutaredoxin class I RNRs Escherichia coli 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + glutaredoxin class I RNRs Lactobacillus leichmannii 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + glutaredoxin class Ia RNRs Homo sapiens 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + glutaredoxin class Ia RNRs Saccharomyces cerevisiae 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + NrdH-redoxin only class Ib RNRs Mus musculus 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + NrdH-redoxin only class Ib RNRs Escherichia coli 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + NrdH-redoxin only class Ib RNRs Lactobacillus leichmannii 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + thioredoxin class I and class II RNRs Mus musculus 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + thioredoxin class I and class II RNRs Escherichia coli 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + thioredoxin class I and class II RNRs Lactobacillus leichmannii 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + thioredoxin class Ia RNRs Homo sapiens 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
nucleoside 5'-diphosphate + thioredoxin class Ia RNRs Saccharomyces cerevisiae 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?

Subunits

Subunits Comment Organism
monomer or dimer alpha or alpha2, class II RNRs Mus musculus
monomer or dimer alpha or alpha2, class II RNRs Escherichia coli
monomer or dimer alpha or alpha2, class II RNRs Lactobacillus leichmannii
More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview 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 Homo sapiens
More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview Saccharomyces cerevisiae
More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview Lactobacillus leichmannii
tetramer alpha2beta2, class I RNRs Mus musculus
tetramer alpha2beta2, class I RNRs Escherichia coli
tetramer alpha2beta2, class I RNRs Homo sapiens
tetramer alpha2beta2, class I RNRs Saccharomyces cerevisiae
tetramer alpha2beta2, class I RNRs Lactobacillus leichmannii

Synonyms

Synonyms Comment Organism
class Ia RNR
-
 Mus musculus
class Ia RNR
-
 Escherichia coli
class Ia RNR
-
 Homo sapiens
class Ia RNR
-
 Saccharomyces cerevisiae
class Ia RNR
-
 Lactobacillus leichmannii
class Ib RNR
-
 Mus musculus
class Ib RNR
-
 Escherichia coli
class Ib RNR
-
 Lactobacillus leichmannii
class II RNR cf. EC 1.17.4.2 Mus musculus
class II RNR cf. EC 1.17.4.2 Escherichia coli
class II RNR cf. EC 1.17.4.2 Lactobacillus leichmannii

Cofactor

Cofactor Comment Organism Structure
5'-deoxyadenosylcobalamin class II enzymes Escherichia coli
Cobalamin class II enzymes Mus musculus
Cobalamin class II enzymes Escherichia coli
Cobalamin class II enzymes Lactobacillus leichmannii
diferric(III)-tyrosyl radical cofactor class I enzymes Mus musculus
diferric(III)-tyrosyl radical cofactor class I enzymes Escherichia coli
diferric(III)-tyrosyl radical cofactor class I enzymes Homo sapiens
diferric(III)-tyrosyl radical cofactor class I enzymes Saccharomyces cerevisiae
diferric(III)-tyrosyl radical cofactor class I enzymes Lactobacillus leichmannii
glutaredoxin class Ia and Ib RNRs Mus musculus
glutaredoxin class Ia and Ib RNRs Escherichia coli
glutaredoxin class Ia and Ib RNRs Lactobacillus leichmannii
glutaredoxin class Ia RNRs Homo sapiens
glutaredoxin class Ia RNRs Saccharomyces cerevisiae
additional information cofactor specificity and binding, role in reaction, overview Mus musculus
additional information cofactor specificity and binding, role in reaction, overview Escherichia coli
additional information cofactor specificity and binding, role in reaction, overview Homo sapiens
additional information cofactor specificity and binding, role in reaction, overview Saccharomyces cerevisiae
additional information cofactor specificity and binding, role in reaction, overview Lactobacillus leichmannii
NrdH-redoxin class Ib RNRs Mus musculus
NrdH-redoxin class Ib RNRs Escherichia coli
NrdH-redoxin class Ib RNRs Lactobacillus leichmannii
thioredoxin class Ia and Ib RNRs and class II RNRs Mus musculus
thioredoxin class Ia and Ib RNRs and class II RNRs Escherichia coli
thioredoxin class Ia and Ib RNRs and class II RNRs Lactobacillus leichmannii
thioredoxin class Ia RNRs Homo sapiens
thioredoxin class Ia RNRs Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information the reaction of class I RNRs involves tyrosyl or cysteinyl radicals and requires aerobic conditions, while for class II RNRs the reaction involves deoxyadenosyl or cysteinyl radicals and is independent of oxygen Mus musculus
additional information the reaction of class I RNRs involves tyrosyl or cysteinyl radicals and requires aerobic conditions, while for class II RNRs the reaction involves deoxyadenosyl or cysteinyl radicals and is independent of oxygen Lactobacillus leichmannii
additional information the reaction of class I RNRs involves tyrosyl or cysteinyl radicals and requires aerobic conditions, while for class II RNRs the 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 the reaction of class Ia RNRs involves tyrosyl or cysteinyl radicals and requires aerobic conditions Homo sapiens
additional information the reaction of class Ia RNRs involves tyrosyl or cysteinyl radicals and requires aerobic conditions Saccharomyces cerevisiae