Literature summary extracted from
Jiang, W.; Xie, J.; Varano, P.T.; Krebs, C.; Bollinger, J.M.
Two distinct mechanisms of inactivation of the class Ic ribonucleotide reductase from Chlamydia trachomatis by hydroxyurea: implications for the protein gating of intersubunit electron transfer (2010), Biochemistry, 49, 5340-5349.
Inhibitors
EC Number |
Inhibitors |
Comment |
Organism |
Structure |
---|
1.17.4.1 |
Hydroxyurea |
inactivates both Ia/b and Ic beta2 subunits by reducing their C oxidants, reacts with the MnIV/FeIII cofactor to give two distinct products: the homogeneous MnIII/FeIII-beta2 complex, which forms only under turnover conditions, in the presence of alpha2 and the substrate, and a distinct, diamagnetic Mn/Fe cluster, which forms about 900fold less rapidly as a second phase in the reaction under turnover conditions and as the sole outcome in the reaction of MnIV/FeIII-beta2 only |
Chlamydia trachomatis |
|
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
1.17.4.1 |
Fe3+ |
MnIV/FeIII cofactor |
Chlamydia trachomatis |
|
1.17.4.1 |
Mn(IV) |
MnIV/FeIII cofactor |
Chlamydia trachomatis |
|
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 |
Chlamydia trachomatis |
catalysis by a class I RNR begins when a cysteine residue in the alpha2 subunit is oxidized to a thiyl radical by a cofactor about 35 A away in the beta2 subunit. In a class Ia or Ib RNR, a stable tyrosyl radical is the C oxidant, whereas a MnIV/FeIII cluster serves this function in the class Ic enzyme from Chlamydia trachomatis |
? |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
1.17.4.1 |
Chlamydia trachomatis |
- |
- |
- |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
1.17.4.1 |
additional information |
catalysis by a class I RNR begins when a cysteine residue in the alpha2 subunit is oxidized to a thiyl radical by a cofactor about 35 A away in the beta2 subunit. In a class Ia or Ib RNR, a stable tyrosyl radical is the C oxidant, whereas a MnIV/FeIII cluster serves this function in the class Ic enzyme from Chlamydia trachomatis |
Chlamydia trachomatis |
? |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
1.17.4.1 |
tetramer |
alpha2beta2, with subunits alpha1, alpha2, beta1, and beta2 |
Chlamydia trachomatis |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
1.17.4.1 |
class I RNR |
- |
Chlamydia trachomatis |
1.17.4.1 |
class Ic ribonucleotide reductase |
- |
Chlamydia trachomatis |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
1.17.4.1 |
MnIV/FeIII cofactor |
electron transfer mechanism and conformational identification, role in reaction and mechanism, detailed overview |
Chlamydia trachomatis |
|