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Literature summary extracted from

  • Jonna, V.R.; Crona, M.; Rofougaran, R.; Lundin, D.; Johansson, S.; Braennstroem, K.; Sjoeberg, B.M.; Hofer, A.
    Diversity in overall activity regulation of ribonucleotide reductase (2015), J. Biol. Chem., 290, 17339-17348 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.17.4.1 ATP activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes Pseudomonas aeruginosa
1.17.4.1 dATP activity of the enzyme is tightly regulated via two allosteric sites, the specificity site (s-site) and the overall activity site (a-site). The a-site resides in an N-terminal ATP cone domain that binds dATP or ATP and functions as an on/off switch, whereas the composite s-site binds ATP, dATP, dTTP, or dGTP and determines which substrate to reduce. The class I ribonucleotide reductase has a duplicated ATP cone domain. Each alpha polypeptide binds three dATP molecules, and the N-terminal ATP cone is critical for binding two of the dATPs because a truncated protein lacking this cone could only bind dATP to its s-site. ATP activates the enzyme solely by preventing dATP from binding. The dATP-induced inactive form is an alpha4 complex, which can interact with beta2 to form a non-productive alpha4beta2 complex. Other allosteric effectors induce a mixture of alpha2 and alpha4 forms, with the former being able to interact with beta2 to form active alpha2beta2 complexes Pseudomonas aeruginosa
1.17.4.1 dTTP only binds to the specificity site (s-site), is able to stimulate tetramer formation Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.1 Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.1 CDP + thioredoxin
-
 Pseudomonas aeruginosa 2'-dCDP + thioredoxin disulfide + H2O
-
 ?

Subunits

EC Number Subunits Comment Organism
1.17.4.1 dimer beta-subunit is predominantly a dimer, whereas the alpha-subunit is in a nucleotide-dependent equilibrium between monomers, dimers, and tetramers. The alpha2beta2 complex is the major active form Pseudomonas aeruginosa
1.17.4.1 monomer beta-subunit is predominantly a dimer, whereas the alpha-subunit is in a nucleotide-dependent equilibrium between monomers, dimers, and tetramers. The alpha2beta2 complex is the major active form Pseudomonas aeruginosa
1.17.4.1 tetramer beta-subunit is predominantly a dimer, whereas the alpha-subunit is in a nucleotide-dependent equilibrium between monomers, dimers, and tetramers. The alpha2beta2 complex is the major active form Pseudomonas aeruginosa

Synonyms

EC Number Synonyms Comment Organism
1.17.4.1 class I ribonucleotide reductase
-
 Pseudomonas aeruginosa
1.17.4.1 class I RNR
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.17.4.1 25
-
 assay at Pseudomonas aeruginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.17.4.1 7.6
-
 assay at Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
1.17.4.1 physiological function the enzyme catalyzes the reduction of ribonucleotides to the corresponding deoxyribonucleotides, which are used as building blocks for DNA replication and repair Pseudomonas aeruginosa