BRENDA - Enzyme Database

Ribonucleotide reductases

Stubbe, J.; Adv. Enzymol. Relat. Areas Mol. Biol. 63, 349-419 (1990)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
1.17.4.1
Herpes simplex virus type I and II
Herpes simplex virus
Engineering
EC Number
Amino acid exchange
Commentary
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
Commentary
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
-
Mus musculus
1.17.4.1
Hydroxyurea
-
Escherichia coli
1.17.4.1
additional information
overview
Escherichia coli
1.17.4.1
additional information
-
Mus musculus
1.17.4.1
additional information
-
Herpes simplex virus
1.17.4.1
nucleotide analogs
overview
Escherichia coli
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.17.4.1
Iron
B2 subunit contains 2 dinuclear Fe3+ centers; iron center is composed of 2 high spin iron atoms antiferromagnetically coupled through a micro-oxo bridge
Escherichia coli
1.17.4.1
Iron
2 iron atoms and a tyrosyl radical per 88000 Da subunit
Mus musculus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.17.4.1
Escherichia coli
-
-
-
1.17.4.1
Herpes simplex virus
-
-
-
1.17.4.1
Mus musculus
-
-
-
Reaction
EC Number
Reaction
Commentary
Organism
1.17.4.1
2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin
postulated mechanism, radical cation intermediates; proposed mechanism
Escherichia coli
1.17.4.1
2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin
postulated mechanism, radical cation intermediates; proposed mechanism
Mus musculus
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.17.4.1
ribonucleoside diphosphate + reduced thioredoxin
-
437936
Mus musculus
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
437936
Mus musculus
ir
1.17.4.1
ribonucleoside diphosphate + reduced thioredoxin
-
437936
Escherichia coli
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
437936
Escherichia coli
ir
1.17.4.1
ribonucleoside diphosphate + reduced thioredoxin
-
437936
Herpes simplex virus
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
437936
Herpes simplex virus
ir
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
1.17.4.1
Herpes simplex virus type I and II
Herpes simplex virus
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
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 (protein specific)
EC Number
Inhibitors
Commentary
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
-
Mus musculus
1.17.4.1
Hydroxyurea
-
Escherichia coli
1.17.4.1
additional information
overview
Escherichia coli
1.17.4.1
additional information
-
Mus musculus
1.17.4.1
additional information
-
Herpes simplex virus
1.17.4.1
nucleotide analogs
overview
Escherichia coli
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.17.4.1
Iron
B2 subunit contains 2 dinuclear Fe3+ centers; iron center is composed of 2 high spin iron atoms antiferromagnetically coupled through a micro-oxo bridge
Escherichia coli
1.17.4.1
Iron
2 iron atoms and a tyrosyl radical per 88000 Da subunit
Mus musculus
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.17.4.1
ribonucleoside diphosphate + reduced thioredoxin
-
437936
Mus musculus
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
437936
Mus musculus
ir
1.17.4.1
ribonucleoside diphosphate + reduced thioredoxin
-
437936
Escherichia coli
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
437936
Escherichia coli
ir
1.17.4.1
ribonucleoside diphosphate + reduced thioredoxin
-
437936
Herpes simplex virus
2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O
-
437936
Herpes simplex virus
ir