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Literature summary extracted from

  • Stubbe, J.
    Ribonucleotide reductases (1990), Adv. Enzymol. Relat. Areas Mol. Biol., 63, 349-419.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.17.4.1 Herpes simplex virus type I and II Herpes simplex virus

Protein Variants

EC Number Protein Variants Comment Organism
1.17.4.1 C225S C225 appears to be one of the participants in the direct reduction of substrate Escherichia coli
1.17.4.1 C759S C759 may play a role in the relay of electrons between thioredoxin and subunit B1 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.4.1 2'-azido-2'-deoxynucleotides
-
 Escherichia coli
1.17.4.1 2'-chloro-2'-deoxycytidine 5'-diphosphate
-
 Escherichia coli
1.17.4.1 2'-halo-2'-deoxynucleotides
-
 Escherichia coli
1.17.4.1 2-azido-UDP rapid time dependent inactivation Escherichia coli
1.17.4.1 3,4,5-Trihydroxybenzohydroxamic acid
-
 Escherichia coli
1.17.4.1 Hydroxyurea
-
 Escherichia coli
1.17.4.1 Hydroxyurea
-
 Mus musculus
1.17.4.1 additional information overview Escherichia coli
1.17.4.1 additional information
-
 Herpes simplex virus
1.17.4.1 additional information
-
 Mus musculus
1.17.4.1 nucleotide analogs overview Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.4.1 Iron 2 iron atoms and a tyrosyl radical per 88000 Da subunit Mus musculus
1.17.4.1 Iron iron center is composed of 2 high spin iron atoms antiferromagnetically coupled through a micro-oxo bridge Escherichia coli
1.17.4.1 Iron B2 subunit contains 2 dinuclear Fe3+ centers Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.1 Escherichia coli
-
-
-
1.17.4.1 Herpes simplex virus
-
-
-
1.17.4.1 Mus musculus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.17.4.1 2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin proposed mechanism Mus musculus
a
1.17.4.1 2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin proposed mechanism Escherichia coli
a
1.17.4.1 2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin postulated mechanism, radical cation intermediates Mus musculus
a
1.17.4.1 2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin postulated mechanism, radical cation intermediates Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.1 ribonucleoside diphosphate + reduced thioredoxin
-
 Mus musculus 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
 ir
1.17.4.1 ribonucleoside diphosphate + reduced thioredoxin
-
 Escherichia coli 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
 ir
1.17.4.1 ribonucleoside diphosphate + reduced thioredoxin
-
 Herpes simplex virus 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
 ir