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Literature summary for 1.17.4.1 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
Search for more literature for 1.17.4.1

Activating Compound

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

Inhibitors

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis JH624
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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]

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
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