Interaction of β-L-Adenosine-5′-triphosphate (L-ATP) with Human Deoxycytidine Kinase, Human DNA Primase and T4 DNA Ligase: Does the Chance Direct Enzymatic Enantioselectivity?

We demonstrate that L-ATP: 1) as well as its natural D-enantiomer, acts as a phosphate donor in the reaction catalysed by human deoxycytidine kinase; 2) inhibits human DNA-primase and the ATP-dependent T4 DNA ligase. Thus, the lack of enantioselectivity of the enzymes is more frequent than it was be...

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Veröffentlicht in:Nucleosides & nucleotides 1999-04, Vol.18 (4-5), p.867-869
Hauptverfasser: Verri, A., Montecucco, A., Gosselin, G., Boudou, V., Spadari, S., Imbach, J-L., Focher, F.
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Sprache:eng
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Zusammenfassung:We demonstrate that L-ATP: 1) as well as its natural D-enantiomer, acts as a phosphate donor in the reaction catalysed by human deoxycytidine kinase; 2) inhibits human DNA-primase and the ATP-dependent T4 DNA ligase. Thus, the lack of enantioselectivity of the enzymes is more frequent than it was believed a few years ago and we suggest that it would depend on chance more than on an evolutionary strategy.
ISSN:0732-8311
DOI:10.1080/15257779908041585