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Literature summary for 1.17.4.1 extracted from

  • Reichard, P.; Eliasson, R.; Ingemarson, R.; Thelander, L.
    Cross-talk between the allosteric effector-binding sites in mouse ribonucleotide reductase (2000), J. Biol. Chem., 275, 33021-33026.
    View publication on PubMed
Search for more literature for 1.17.4.1

Activating Compound

Activating Compound Comment Organism Structure
ATP required for CDP reduction Mus musculus
dATP stimulation of ADP reduction Mus musculus
dATP 6fold stimulation of GDP reduction Mus musculus
dGTP required for ADP reduction Mus musculus
dTTP required for GDP reduction Mus musculus
additional information subunit R1 has 2 effector-binding sites per polypeptide chain: one activity site for dATP and ATP, with dATP-inhibiting and ATP-stimulating catalytic activity and a second specificity site for dATP, ATP, dTTP and dGTP directing substrate specificity Mus musculus

Protein Variants

Protein Variants Comment Organism
D57N mutation in R1 subunit, in contrast to wild-type dATP stimulates CDP reduction, GDP reduction is inhibited by dGTP, ADP reduction is inhibited by dTTP similar to wild-type, this suggests that the mutant enzyme binds both ATP and dATP to the activity site but does not distinguish between them when it comes to catalysis Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
dATP strong inhibition of the ATP activated enzyme, complete inhibition of GDP reduction, inhibition of ADP reduction Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2'-deoxyribonucleoside 5'-diphosphate + thioredoxin disulfide + H2O = ribonucleoside 5'-diphosphate + thioredoxin allosteric regulation of the catalytic activity of subunit R1 Mus musculus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ribonucleoside diphosphate + reduced thioredoxin
-
 Mus musculus 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H2O CDP, ADP and GDP are reduced very poorly in the absence of allosteric effectors ir