Human ribonucleotide reductase. Activation and inhibition by analogs of ATP.

Article Details

Citation

Harrington JA, Spector T

Human ribonucleotide reductase. Activation and inhibition by analogs of ATP.

Biochem Pharmacol. 1991 Jul 25;42(4):759-63.

PubMed ID
1867633 [ View in PubMed
]
Abstract

Sixteen ATP analogs were studied as activators of CDP reduction catalyzed by human ribonucleotide reductase. Activation constants were determined. Three analogs, 3-deazaATP, 5'-adenylimidodiphosphate, and 3'-dATP, activated approximately as efficiently as ATP. Four analogs were partial activators. These seven activators were also accessory activators of GDP reduction. Furthermore, two other analogs, adenosine-5'-O-(1-thiotriphosphate) and 8-bromoATP, selectively stimulated GDP reduction. Ten analogs, at equal molar concentrations with ATP, inhibited ATP-dependent activation of CDP reduction and/or accessory activation of GDP reduction by greater than 45%. No analog inhibited as potently as 2'-dATP, which had an IC50 of 30-50 microM versus the stimulation of CDP and GDP reduction by 2.0 mM ATP.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Ribonucleoside-diphosphate reductase large subunitP23921Details