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Literature summary for 1.17.4.1 extracted from

  • Stubbe, J.
    Ribonucleotide reductases (1990), Adv. Enzymol. Relat. Areas Mol. Biol., 63, 349-419.
    View publication on PubMed
Search for more literature for 1.17.4.1

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

Metals/Ions

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

Organism

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

Reaction

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

Substrates and Products (Substrate)

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