BRENDA - Enzyme Database

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

Jiang, W.; Xie, J.; Varano, P.T.; Krebs, C.; Bollinger, J.M.; Biochemistry 49, 5340-5349 (2010)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
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
Commentary
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
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
1.17.4.1
Chlamydia trachomatis
-
-
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
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
714196
Chlamydia trachomatis
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
1.17.4.1
tetramer
alpha2beta2, with subunits alpha1, alpha2, beta1, and beta2
Chlamydia trachomatis
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.17.4.1
MnIV/FeIII cofactor
electron transfer mechanism and conformational identification, role in reaction and mechanism, detailed overview
Chlamydia trachomatis
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.17.4.1
MnIV/FeIII cofactor
electron transfer mechanism and conformational identification, role in reaction and mechanism, detailed overview
Chlamydia trachomatis
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
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 (protein specific)
EC Number
Metals/Ions
Commentary
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) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
?
-
-
-
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
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
714196
Chlamydia trachomatis
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.17.4.1
tetramer
alpha2beta2, with subunits alpha1, alpha2, beta1, and beta2
Chlamydia trachomatis