BRENDA - Enzyme Database

Redox intermediates of the Mn-Fe Site in subunit R2 of Chlamydia trachomatis ribonucleotide reductase: an X-ray absorption and EPR study

Voevodskaya, N.; Lendzian, F.; Sanganas, O.; Grundmeier, A.; Graeslund, A.; Haumann, M.; J. Biol. Chem. 284, 4555-4566 (2009)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
1.17.4.1
ATP
-
Chlamydia trachomatis
1.17.4.1
additional information
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
Chlamydia trachomatis
Crystallization (Commentary)
EC Number
Crystallization
Organism
1.17.4.1
subunit R2, X-ray diffraction structure determination and analysis at 2.75-2.90 A resolution
Chlamydia trachomatis
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.17.4.1
Hydroxyurea
-
Chlamydia trachomatis
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
1.17.4.1
Fe2+
metal content determination of oxidized and reduced subunit R2, electronic features and nuclear geometry of the manganese and iron sites, kinetics, overview. 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. Structure modelling
Chlamydia trachomatis
1.17.4.1
Mg2+
activates
Chlamydia trachomatis
1.17.4.1
Mn2+
metal content determination of oxidized and reduced subunit R2, electronic features and nuclear geometry of the manganese and iron sites, kinetics, overview. 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. Structure modelling
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
substrate is CDP, R2 is the catalytic subunit
704612
Chlamydia trachomatis
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
1.17.4.1
heterotetramer
R1R2 complex
Chlamydia trachomatis
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.17.4.1
22
-
assay at room temperature
Chlamydia trachomatis
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.17.4.1
Mn-Fe cofactor
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
Chlamydia trachomatis
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
1.17.4.1
ATP
-
Chlamydia trachomatis
1.17.4.1
additional information
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
Chlamydia trachomatis
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.17.4.1
Mn-Fe cofactor
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
Chlamydia trachomatis
Crystallization (Commentary) (protein specific)
EC Number
Crystallization
Organism
1.17.4.1
subunit R2, X-ray diffraction structure determination and analysis at 2.75-2.90 A resolution
Chlamydia trachomatis
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.17.4.1
Hydroxyurea
-
Chlamydia trachomatis
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
1.17.4.1
Fe2+
metal content determination of oxidized and reduced subunit R2, electronic features and nuclear geometry of the manganese and iron sites, kinetics, overview. 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. Structure modelling
Chlamydia trachomatis
1.17.4.1
Mg2+
activates
Chlamydia trachomatis
1.17.4.1
Mn2+
metal content determination of oxidized and reduced subunit R2, electronic features and nuclear geometry of the manganese and iron sites, kinetics, overview. 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. Structure modelling
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
substrate is CDP, R2 is the catalytic subunit
704612
Chlamydia trachomatis
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.17.4.1
heterotetramer
R1R2 complex
Chlamydia trachomatis
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
1.17.4.1
22
-
assay at room temperature
Chlamydia trachomatis