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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.4.1 caracemide
-
 Escherichia coli
1.17.4.1 caracemide
-
 Homo sapiens
1.17.4.1 caracemide
-
 Lactobacillus leichmannii
1.17.4.1 caracemide
-
 Mus musculus
1.17.4.1 caracemide
-
 Saccharomyces cerevisiae
1.17.4.1 chlorambucil
-
 Escherichia coli
1.17.4.1 chlorambucil
-
 Homo sapiens
1.17.4.1 chlorambucil
-
 Lactobacillus leichmannii
1.17.4.1 chlorambucil
-
 Mus musculus
1.17.4.1 chlorambucil
-
 Saccharomyces cerevisiae
1.17.4.1 cisplatin
-
 Escherichia coli
1.17.4.1 cisplatin
-
 Homo sapiens
1.17.4.1 cisplatin
-
 Lactobacillus leichmannii
1.17.4.1 cisplatin
-
 Mus musculus
1.17.4.1 cisplatin
-
 Saccharomyces cerevisiae
1.17.4.1 Co2+ RNR activity chelates with copper leading to inactivation Escherichia coli
1.17.4.1 Co2+ RNR activity chelates with copper leading to inactivation Homo sapiens
1.17.4.1 Co2+ RNR activity chelates with copper leading to inactivation Lactobacillus leichmannii
1.17.4.1 Co2+ RNR activity chelates with copper leading to inactivation Mus musculus
1.17.4.1 Co2+ RNR activity chelates with copper leading to inactivation Saccharomyces cerevisiae
1.17.4.2 caracemide
-
 Escherichia coli
1.17.4.2 caracemide
-
 Mus musculus
1.17.4.2 caracemide
-
 Tequatrovirus T4
1.17.4.2 chlorambucil
-
 Escherichia coli
1.17.4.2 chlorambucil
-
 Mus musculus
1.17.4.2 chlorambucil
-
 Tequatrovirus T4
1.17.4.2 cisplatin
-
 Escherichia coli
1.17.4.2 cisplatin
-
 Mus musculus
1.17.4.2 cisplatin
-
 Tequatrovirus T4
1.17.4.2 Co2+ RNR activity chelates with copper leading to inactivation Escherichia coli
1.17.4.2 Co2+ RNR activity chelates with copper leading to inactivation Mus musculus
1.17.4.2 Co2+ RNR activity chelates with copper leading to inactivation Tequatrovirus T4

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.4.1 Co2+ class II enzymes contain cobalamin as cofactor Mus musculus
1.17.4.1 Co2+ class II enzymes contain cobalamin as cofactor Escherichia coli
1.17.4.1 Co2+ class II enzymes contain cobalamin as cofactor Lactobacillus leichmannii
1.17.4.1 Fe class I enzymes contain diferric(III)-tyrosyl radical cofactor Escherichia coli
1.17.4.1 Fe3+ class I enzymes contain diferric(III)-tyrosyl radical cofactor Mus musculus
1.17.4.1 Fe3+ class I enzymes contain diferric(III)-tyrosyl radical cofactor Homo sapiens
1.17.4.1 Fe3+ class I enzymes contain diferric(III)-tyrosyl radical cofactor Saccharomyces cerevisiae
1.17.4.1 Fe3+ class I enzymes contain diferric(III)-tyrosyl radical cofactor Lactobacillus leichmannii
1.17.4.2 Co2+ class II enzymes contain cobalamin as cofactor Mus musculus
1.17.4.2 Co2+ class II enzymes contain cobalamin as cofactor Escherichia coli
1.17.4.2 Fe2+ the class III enzymes contain 4Fe-4S clusters in the small beta-subunit Escherichia coli
1.17.4.2 Fe2+ the class III enzymes contain 4Fe-4S clusters in the small beta-subunit Tequatrovirus T4

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.4.1 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 ?
-
 ?
1.17.4.1 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 ?
-
 ?
1.17.4.1 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 ?
-
 ?
1.17.4.1 additional information Homo sapiens class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor ?
-
 ?
1.17.4.1 additional information Saccharomyces cerevisiae class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor ?
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + glutaredoxin Mus musculus class I RNRs 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + glutaredoxin Escherichia coli class I RNRs 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + glutaredoxin Lactobacillus leichmannii class I RNRs 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + glutaredoxin Homo sapiens class Ia RNRs 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + glutaredoxin Saccharomyces cerevisiae class Ia RNRs 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + NrdH-redoxin Mus musculus only class Ib RNRs 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + NrdH-redoxin Escherichia coli only class Ib RNRs 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + NrdH-redoxin Lactobacillus leichmannii only class Ib RNRs 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + thioredoxin Mus musculus class I and class II RNRs 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + thioredoxin Escherichia coli class I and class II RNRs 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + thioredoxin Lactobacillus leichmannii class I and class II RNRs 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + thioredoxin Homo sapiens class Ia RNRs 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + thioredoxin Saccharomyces cerevisiae class Ia RNRs 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.2 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 ?
-
 ?
1.17.4.2 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 ?
-
 ?
1.17.4.2 nucleoside 5'-triphosphate + formate Escherichia coli class III RNR 2'-deoxynucleoside 5'-triphosphate + H2O
-
 ?
1.17.4.2 nucleoside 5'-triphosphate + formate Tequatrovirus T4 class III RNR 2'-deoxynucleoside 5'-triphosphate + H2O
-
 ?
1.17.4.2 nucleoside 5'-triphosphate + thioredoxin Mus musculus class II RNRs 2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.2 nucleoside 5'-triphosphate + thioredoxin Escherichia coli class II RNRs 2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.1 Escherichia coli
-
-
-
1.17.4.1 Homo sapiens
-
-
-
1.17.4.1 Lactobacillus leichmannii
-
-
-
1.17.4.1 Mus musculus
-
-
-
1.17.4.1 Saccharomyces cerevisiae
-
-
-
1.17.4.2 Escherichia coli
-
-
-
1.17.4.2 Mus musculus
-
-
-
1.17.4.2 Tequatrovirus T4
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.1 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 ?
-
 ?
1.17.4.1 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 ?
-
 ?
1.17.4.1 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 ?
-
 ?
1.17.4.1 additional information class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor Homo sapiens ?
-
 ?
1.17.4.1 additional information class Ia RNRs convert nucleoside diphosphates into 2'-deoxynucleoside diphosphates using glutaredoxin or thioredoxin as cofactor Saccharomyces cerevisiae ?
-
 ?
1.17.4.1 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 ?
-
 ?
1.17.4.1 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 ?
-
 ?
1.17.4.1 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 ?
-
 ?
1.17.4.1 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 ?
-
 ?
1.17.4.1 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 ?
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + glutaredoxin class I RNRs Mus musculus 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + glutaredoxin class I RNRs Escherichia coli 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + glutaredoxin class I RNRs Lactobacillus leichmannii 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + glutaredoxin class Ia RNRs Homo sapiens 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + glutaredoxin class Ia RNRs Saccharomyces cerevisiae 2'-deoxynucleoside 5'-diphosphate + glutaredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + NrdH-redoxin only class Ib RNRs Mus musculus 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + NrdH-redoxin only class Ib RNRs Escherichia coli 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + NrdH-redoxin only class Ib RNRs Lactobacillus leichmannii 2'-deoxynucleoside 5'-diphosphate + NrdH-redoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + thioredoxin class I and class II RNRs Mus musculus 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + thioredoxin class I and class II RNRs Escherichia coli 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + thioredoxin class I and class II RNRs Lactobacillus leichmannii 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + thioredoxin class Ia RNRs Homo sapiens 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.1 nucleoside 5'-diphosphate + thioredoxin class Ia RNRs Saccharomyces cerevisiae 2'-deoxynucleoside 5'-diphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.2 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 Escherichia coli ?
-
 ?
1.17.4.2 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 Mus musculus ?
-
 ?
1.17.4.2 additional information the class II RNR also uses nucleoside 5'-diphosphate as substrate Mus musculus ?
-
 ?
1.17.4.2 additional information the class II RNR also uses nucleoside 5'-diphosphate as substrate Escherichia coli ?
-
 ?
1.17.4.2 nucleoside 5'-triphosphate + formate class III RNR Escherichia coli 2'-deoxynucleoside 5'-triphosphate + H2O
-
 ?
1.17.4.2 nucleoside 5'-triphosphate + formate class III RNR Tequatrovirus T4 2'-deoxynucleoside 5'-triphosphate + H2O
-
 ?
1.17.4.2 nucleoside 5'-triphosphate + thioredoxin class II RNRs Mus musculus 2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
 ?
1.17.4.2 nucleoside 5'-triphosphate + thioredoxin class II RNRs Escherichia coli 2'-deoxynucleoside 5'-triphosphate + thioredoxin disulfide + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.17.4.1 monomer or dimer alpha or alpha2, class II RNRs Mus musculus
1.17.4.1 monomer or dimer alpha or alpha2, class II RNRs Escherichia coli
1.17.4.1 monomer or dimer alpha or alpha2, class II RNRs Lactobacillus leichmannii
1.17.4.1 More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview Mus musculus
1.17.4.1 More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview Escherichia coli
1.17.4.1 More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview Homo sapiens
1.17.4.1 More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview Saccharomyces cerevisiae
1.17.4.1 More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview Lactobacillus leichmannii
1.17.4.1 tetramer alpha2beta2, class I RNRs Mus musculus
1.17.4.1 tetramer alpha2beta2, class I RNRs Escherichia coli
1.17.4.1 tetramer alpha2beta2, class I RNRs Homo sapiens
1.17.4.1 tetramer alpha2beta2, class I RNRs Saccharomyces cerevisiae
1.17.4.1 tetramer alpha2beta2, class I RNRs Lactobacillus leichmannii
1.17.4.2 monomer or dimer alpha or alpha2, class II RNRs Mus musculus
1.17.4.2 monomer or dimer alpha or alpha2, class II RNRs Escherichia coli
1.17.4.2 More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview Mus musculus
1.17.4.2 More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview Escherichia coli
1.17.4.2 More structure comparisons of classI-III RNRs, model for the subunit organization of RNRs, overview Tequatrovirus T4
1.17.4.2 tetramer alpha2beta2, class III RNRs Escherichia coli
1.17.4.2 tetramer alpha2beta2, class III RNRs Tequatrovirus T4

Synonyms

EC Number Synonyms Comment Organism
1.17.4.1 class Ia RNR
-
 Mus musculus
1.17.4.1 class Ia RNR
-
 Escherichia coli
1.17.4.1 class Ia RNR
-
 Homo sapiens
1.17.4.1 class Ia RNR
-
 Saccharomyces cerevisiae
1.17.4.1 class Ia RNR
-
 Lactobacillus leichmannii
1.17.4.1 class Ib RNR
-
 Mus musculus
1.17.4.1 class Ib RNR
-
 Escherichia coli
1.17.4.1 class Ib RNR
-
 Lactobacillus leichmannii
1.17.4.1 class II RNR cf. EC 1.17.4.2 Mus musculus
1.17.4.1 class II RNR cf. EC 1.17.4.2 Escherichia coli
1.17.4.1 class II RNR cf. EC 1.17.4.2 Lactobacillus leichmannii
1.17.4.2 class II RNR cf. EC 1.17.4.1 Mus musculus
1.17.4.2 class II RNR cf. EC 1.17.4.1 Escherichia coli
1.17.4.2 class III RNR
-
 Escherichia coli
1.17.4.2 class III RNR
-
 Tequatrovirus T4

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.4.1 5'-deoxyadenosylcobalamin class II enzymes Escherichia coli
1.17.4.1 Cobalamin class II enzymes Mus musculus
1.17.4.1 Cobalamin class II enzymes Escherichia coli
1.17.4.1 Cobalamin class II enzymes Lactobacillus leichmannii
1.17.4.1 diferric(III)-tyrosyl radical cofactor class I enzymes Mus musculus
1.17.4.1 diferric(III)-tyrosyl radical cofactor class I enzymes Escherichia coli
1.17.4.1 diferric(III)-tyrosyl radical cofactor class I enzymes Homo sapiens
1.17.4.1 diferric(III)-tyrosyl radical cofactor class I enzymes Saccharomyces cerevisiae
1.17.4.1 diferric(III)-tyrosyl radical cofactor class I enzymes Lactobacillus leichmannii
1.17.4.1 glutaredoxin class Ia and Ib RNRs Mus musculus
1.17.4.1 glutaredoxin class Ia and Ib RNRs Escherichia coli
1.17.4.1 glutaredoxin class Ia and Ib RNRs Lactobacillus leichmannii
1.17.4.1 glutaredoxin class Ia RNRs Homo sapiens
1.17.4.1 glutaredoxin class Ia RNRs Saccharomyces cerevisiae
1.17.4.1 additional information cofactor specificity and binding, role in reaction, overview Mus musculus
1.17.4.1 additional information cofactor specificity and binding, role in reaction, overview Escherichia coli
1.17.4.1 additional information cofactor specificity and binding, role in reaction, overview Homo sapiens
1.17.4.1 additional information cofactor specificity and binding, role in reaction, overview Saccharomyces cerevisiae
1.17.4.1 additional information cofactor specificity and binding, role in reaction, overview Lactobacillus leichmannii
1.17.4.1 NrdH-redoxin class Ib RNRs Mus musculus
1.17.4.1 NrdH-redoxin class Ib RNRs Escherichia coli
1.17.4.1 NrdH-redoxin class Ib RNRs Lactobacillus leichmannii
1.17.4.1 thioredoxin class Ia and Ib RNRs and class II RNRs Mus musculus
1.17.4.1 thioredoxin class Ia and Ib RNRs and class II RNRs Escherichia coli
1.17.4.1 thioredoxin class Ia and Ib RNRs and class II RNRs Lactobacillus leichmannii
1.17.4.1 thioredoxin class Ia RNRs Homo sapiens
1.17.4.1 thioredoxin class Ia RNRs Saccharomyces cerevisiae
1.17.4.2 5'-deoxyadenosylcobalamin class II enzymes Mus musculus
1.17.4.2 5'-deoxyadenosylcobalamin class II enzymes Escherichia coli
1.17.4.2 Cobalamin class II enzymes Mus musculus
1.17.4.2 Cobalamin class II enzymes Escherichia coli
1.17.4.2 additional information cofactor specificity and binding, role in reaction, overview Mus musculus
1.17.4.2 additional information cofactor specificity and binding, role in reaction, overview Escherichia coli
1.17.4.2 additional information the class III enzymes contain 4Fe-4S clusters in the small beta-subunit. Cofactor specificity and binding, role in reaction, overview Escherichia coli
1.17.4.2 additional information the class III enzymes contain 4Fe-4S clusters in the small beta-subunit. Cofactor specificity and binding, role in reaction, overview Tequatrovirus T4
1.17.4.2 S-adenosyl-L-methionine
-
 Escherichia coli
1.17.4.2 S-adenosyl-L-methionine
-
 Tequatrovirus T4
1.17.4.2 thioredoxin
-
 Escherichia coli
1.17.4.2 thioredoxin class II enzymes Mus musculus

General Information

EC Number General Information Comment Organism
1.17.4.1 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
1.17.4.1 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
1.17.4.1 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
1.17.4.1 additional information the reaction of class Ia RNRs involves tyrosyl or cysteinyl radicals and requires aerobic conditions Homo sapiens
1.17.4.1 additional information the reaction of class Ia RNRs involves tyrosyl or cysteinyl radicals and requires aerobic conditions Saccharomyces cerevisiae
1.17.4.2 additional information Cys290 in class III from bacteriophage T4 are the conserved cysteine residues that are the sites for generation of the thiyl radical Tequatrovirus T4
1.17.4.2 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
1.17.4.2 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 Escherichia coli
1.17.4.2 additional information the class III RNR reaction involves deoxyadenosyl, glycyl, or cysteinyl radicals and requires anaerobic conditions Escherichia coli
1.17.4.2 physiological function during anaerobic growth, Escherichia coli depends on a class III RNR for the synthesis of deoxyribonucleotides Escherichia coli