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Literature summary extracted from

  • Voevodskaya, N.; Lendzian, F.; Sanganas, O.; Grundmeier, A.; Graeslund, A.; Haumann, M.
    Redox intermediates of the Mn-Fe Site in subunit R2 of Chlamydia trachomatis ribonucleotide reductase: an X-ray absorption and EPR study (2009), J. Biol. Chem., 284, 4555-4566.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment 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 (Comment) 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 Comment Organism Structure
1.17.4.1 Hydroxyurea
-
 Chlamydia trachomatis

Metals/Ions

EC Number Metals/Ions Comment 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 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 substrate is CDP, R2 is the catalytic subunit Chlamydia trachomatis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.17.4.1 heterotetramer R1R2 complex Chlamydia trachomatis

Synonyms

EC Number Synonyms Comment Organism
1.17.4.1 class I ribonucleotide reductase
-
 Chlamydia trachomatis
1.17.4.1 ribonucleotide reductase
-
 Chlamydia trachomatis
1.17.4.1 RNR
-
 Chlamydia trachomatis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.17.4.1 22
-
 assay at room temperature Chlamydia trachomatis

Cofactor

EC Number Cofactor Comment 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