1.17.4.1: ribonucleoside-diphosphate reductase
This is an abbreviated version!
For detailed information about ribonucleoside-diphosphate reductase, go to the full flat file.
Word Map on EC 1.17.4.1
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1.17.4.1
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deoxyribonucleotides
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hydroxyurea
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tyrosyl
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reductases
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chlamydia
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trachomatis
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deoxynucleotides
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proton-coupled
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diiron
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deoxycytidine
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diferric
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thiyl
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dntps
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dcdp
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thiosemicarbazone
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diferric-tyrosyl
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nrdabs
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hydroxyurea-resistant
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medicine
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nrdef
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heterodinuclear
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drug development
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antiferromagnetically
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pharmacology
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molecular biology
- 1.17.4.1
- deoxyribonucleotides
- hydroxyurea
-
tyrosyl
- reductases
- chlamydia
- trachomatis
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deoxynucleotides
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proton-coupled
-
diiron
- deoxycytidine
-
diferric
-
thiyl
- dntps
- dcdp
- thiosemicarbazone
-
diferric-tyrosyl
-
nrdabs
-
hydroxyurea-resistant
- medicine
-
nrdef
-
heterodinuclear
- drug development
-
antiferromagnetically
- pharmacology
- molecular biology
Reaction
Synonyms
2'-deoxyribonucleoside-diphosphate:oxidized-thioredoxin 2'-oxidoreductase, ADP reductase, CDP reductase, class I ribonucleotide reductase, class I ribonulceotide reductase, class I RNR, class I RR, class Ia ribonucleotide reductase, class Ia RNR, class Ia RR, class Ib ribonucleotide reductase, class Ib RNR, class Ic ribonucleotide reductase, class II RNR, manganese-ribonucleotide reductase, Mn-RNR, More, mRR, NrdA, NrdB, NrdE, NrdF, nucleoside diphosphate reductase, p53-inducible ribonucleotide reductase, R2F, reductase, ribonucleoside diphosphate, ribonucleoside 5'-diphosphate reductase, ribonucleoside diphosphate reductase, ribonucleoside-diphosphate reductase subunit M2 B, ribonucleotide diphosphate reductase, ribonucleotide reductase, RIR1, RIR2, RNR, RNR1 rRibonucleoside-diphosphate reductase large chain 1, RNR2, UDP reductase
ECTree
1.17.4.1 ribonucleoside-diphosphate reductaseAdvanced search results
results (
results (Cofactor
Cofactor on EC 1.17.4.1 - ribonucleoside-diphosphate reductase
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COFACTOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
adenosylcobalamin
absolutely requires adenosylcobalamin (as a radical generator) for activity, KM: 0.001 mM
dimanganese-tyrosyl radical cofactor
the enzyme uses a dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor in vivo. The dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor is 3.5fold more active than the iron form. The flavodoxin NrdI is essential for assembly of the ribonucleotide reductase metallo-cofactor
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Fe2 III/III-Y radical cofactor
assembly, maintenance, and role in catalysis of the Fe2 III/III-Y radical cofactor of Ecbeta2 subunit, structure modelling, detailed overview
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FMN
binding structure analysis with NrdF and NrdI, NrdF contributes to the electrostatic environment of the FMN binding pocket, overview
Mn-Fe cofactor
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the R2 protein of class I RNR contains a Mn-Fe instead of the standard Fe-Fe cofactor. Ct R2 has a redox-inert phenylalanine replacing the radical-forming tyrosine of classic RNRs, which implies a different mechanism of O2 activation, overview
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Mn/Fe redox cofactor
unusual cofactor instead of Fe-Fe cofactor in other RNRs. Assembly, maintenance, and role in catalysis of the MnIV/FeIII cofactor of Ctbeta2 subunit, structure modelling, detailed overview
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MnIV/FeIII cofactor
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electron transfer mechanism and conformational identification, role in reaction and mechanism, detailed overview
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diferric(III)-tyrosyl radical cofactor
an active diiron-tyrosyl radical cofactor is present in the the R2F-1 small subunit
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diferric(III)-tyrosyl radical cofactor
the dimanganese-tyrosyl radical (Mn(III)2-Y(*)) cofactor is 3.5fold more active than the iron form. The flavodoxin NrdI is essential for assembly of the ribonucleotide reductase metallo-cofactor
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dimanganese(III)-tyrosyl radical cofactor
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MnIII2-tyrosyl radical cofactor
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dimanganese(III)-tyrosyl radical cofactor
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the dimanganese(III)-tyrosyl radical cofactor, not the diferric-tyrosyl radical one, is the active metallocofactor in vivo
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manganese-iron cofactor
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the class Ic RNR from Chlamydia trachomatis uses a Mn(IV)/Fe(III) cofactor, with high specificity for MnIV, which functionally replaces the tyrosyl radical used by conventional class I RNRs to initiate substrate radical production. The intermediate decays by reduction of the Fe site to the active MnIV/FeIII-R2 complex. The reaction of the MnII/FeII-R2 species with H2O2 proceeds in three resolved steps: sequential oxidation to MnIII/FeIII-R2 and Mn(IV)/Fe(IV)-R2, followed by decay of the intermediate to the active Mn(IV)/Fe(III)-R2 product, kinetics and reaction mechanism, overview
manganese-iron cofactor
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the class Ic RNR from Chlamydia trachomatis uses a MnIV/FeIII cofactor, with high specificity for MnIV in place of the tyrosyl radical for radical initiation, R2 is activated when its MnII/FeII form reacts with O2 to generate a MnIV/FeIV intermediate, which decays by reduction of the FeIV site to the active MnIV/FeIII state, the reduction step in this sequence is mediated by residue Y222, overview
T4 thioredoxin
Tequatrovirus T4
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enzyme induced in E. coli by infection with bacteriophage T4
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additional information
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analysis of composition and conformation, and of the reaction mechanism of the metallo-cofactor, detailed overview
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additional information
class Ib ribonucleotide reductase can initiate reduction of nucleotides to deoxynucleotides with either a MnIII 2-tyrosyl radical or a FeIII 2-tyrosyl radical cofactor in the NrdF subunit. Whereas FeIII 2-tyrosyl radical can self-assemble from FeII 2-NrdF and O2, activation of MnII 2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2
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additional information
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cofactor specificity and binding, role in reaction, overview
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additional information
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cofactor specificity and binding, role in reaction, overview
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additional information
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cofactor specificity and binding, role in reaction, overview
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additional information
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cofactor specificity and binding, role in reaction, overview
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additional information
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cofactor specificity and binding, role in reaction, overview
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additional information
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metal cofactor composition and conformation analysis, complex stabilities and geometries, calculations and modelling of enzyme geometries including cofactors and active site, detailed overview
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additional information
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RNR is active with both FeIII2-tyrosyl radical and MnIII2-tyrosyl radical cofactors in the beta2 subunit, NrdF
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