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Literature summary for 1.17.4.2 extracted from

  • Arnaoutov, A.; Dasso, M.
    Enzyme regulation. IRBIT is a novel regulator of ribonucleotide reductase in higher eukaryotes (2014), Science, 345, 1512-1515 .
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
IRBIT IRBIT is a conserved metazoan protein implicated in diverse functions. IRBIT consists of a putative enzymatic domain that has similarity to S-adenosylhomocysteine hydrolase and an essential N-terminal domain of 104 amino acids. It forms a dATP-dependent complex with ribonucleotide reductase, which stabilizes dATP in the activity site of ribonucleotide reductase and thus inhibits the enzyme. Formation of the ribonucleotide reductase-IRBIT complex is regulated through phosphorylation of IRBIT, and ablation of IRBIT expression in HeLa cells causes imbalanced dNTP pools and altered cell cycle progression. Under normal physiological conditions, where ATP levels are high, such inhibition can only be achieved when binding of IRBIT is strengthened by phosphorylation Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
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Homo sapiens
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