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Literature summary for 1.17.4.1 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
Search for more literature for 1.17.4.1

Activating Compound

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

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms Comment Organism
class I ribonucleotide reductase
-
 Pseudomonas aeruginosa
class I RNR
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

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

pH Optimum

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

General Information

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