Activating Compound | Comment | Organism | Structure |
---|---|---|---|
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 | |
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 | |
dTTP | only binds to the specificity site (s-site), is able to stimulate tetramer formation | Pseudomonas aeruginosa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
CDP + thioredoxin | - |
Pseudomonas aeruginosa | 2'-dCDP + thioredoxin disulfide + H2O | - |
? |
Subunits | Comment | Organism |
---|---|---|
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 |
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 |
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 | Comment | Organism |
---|---|---|
class I ribonucleotide reductase | - |
Pseudomonas aeruginosa |
class I RNR | - |
Pseudomonas aeruginosa |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Pseudomonas aeruginosa |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.6 | - |
assay at | Pseudomonas aeruginosa |
General Information | Comment | Organism |
---|---|---|
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 |