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Literature summary extracted from

  • Parker, M.J.; Zhu, X.; Stubbe, J.
    Bacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions (2014), Biochemistry, 53, 766-776.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.17.4.1 ATP ATP maximally stimulates CDP reduction at 1.5 mM Bacillus subtilis
1.17.4.1 dATP dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.4.1 dATP dATP maximally stimulates CDP reduction at 8-10 microM followed by rapid inhibition at higher concentrations Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.4.1 Iron may substitute or manganese Bacillus subtilis
1.17.4.1 Manganese dimanganic-tyrosyl radical cofactor Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.17.4.1 49600
-
isolated subunit NrdF, plus major fraction of 80100 Dalton, gel filtration Bacillus subtilis
1.17.4.1 80100
-
isolated subunit NrdF, plus small fraction of 49600 Dalton, gel filtration Bacillus subtilis
1.17.4.1 82700
-
isolated subunit NrdE Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.1 Bacillus subtilis
-
-
-
1.17.4.1 Bacillus subtilis JH624
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.4.1 isolation of beta-subunit NrdF using anion exchange chromatography to separate apo-/mismetalated-NrdFs from dimanganic-tyrosyl radical cofactor Bacillus subtilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.17.4.1 52
-
iron-loaded enzyme, cosubstrate dithiothreitol, presence of 3 mM ATP, pH 7.6, 37°C Bacillus subtilis
1.17.4.1 106
-
iron-loaded enzyme, cosubstrate thioredoxin YosR, presence of 3 mM ATP, pH 7.6, 37°C Bacillus subtilis
1.17.4.1 125
-
iron-loaded enzyme, cosubstrate thioredoxin A, presence of 3 mM ATP, pH 7.6, 37°C Bacillus subtilis
1.17.4.1 146
-
manganese-loaded enzyme, cosubstrate dithiothreitol, presence of 3 mM ATP, pH 7.6, 37°C Bacillus subtilis
1.17.4.1 997
-
manganese-loaded enzyme, cosubstrate thioredoxin YosR, presence of 3 mM ATP, pH 7.6, 37°C Bacillus subtilis
1.17.4.1 1475
-
manganese-loaded enzyme, cosubstrate thioredoxin A, presence of 3 mM ATP, pH 7.6, 37°C Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.1 CDP + dithiothreitol
-
Bacillus subtilis 2'-dCDP + oxidized dithiothreitol + H2O
-
?
1.17.4.1 CDP + dithiothreitol
-
Bacillus subtilis JH624 2'-dCDP + oxidized dithiothreitol + H2O
-
?
1.17.4.1 CDP + thioredoxin A
-
Bacillus subtilis 2'-dCDP + thioredoxin A disulfide + H2O
-
?
1.17.4.1 CDP + thioredoxin A
-
Bacillus subtilis JH624 2'-dCDP + thioredoxin A disulfide + H2O
-
?
1.17.4.1 CDP + thioredoxin YosR
-
Bacillus subtilis 2'-dCDP + thioredoxin YosR disulfide + H2O
-
?
1.17.4.1 CDP + thioredoxin YosR
-
Bacillus subtilis JH624 2'-dCDP + thioredoxin YosR disulfide + H2O
-
?
1.17.4.1 additional information Bacillus subtilis ribonucleotide reductase can be assayed as a holo-enzyme by using equivalent amounts of each subunit Bacillus subtilis ?
-
?
1.17.4.1 additional information Bacillus subtilis ribonucleotide reductase can be assayed as a holo-enzyme by using equivalent amounts of each subunit Bacillus subtilis JH624 ?
-
?

Subunits

EC Number Subunits Comment Organism
1.17.4.1 More at physiological concentrations, alpha-subunit NrdE is a monomer and beta-subunit NrdF in complex with dimanganic-tyrosyl radical cofactor is a dimer. A 1:1 mixture of NrdE:NrdF, however, is composed of a complex mixture of structures Bacillus subtilis