Interaction of beta-L-adenosine-5 '-triphosphate (L-ATP) with human deoxycytidine kinase, human DNA primase and T4 DNA ligase: Does the chance directenzymatic enantioselectivity?
A. Verri et al., Interaction of beta-L-adenosine-5 '-triphosphate (L-ATP) with human deoxycytidine kinase, human DNA primase and T4 DNA ligase: Does the chance directenzymatic enantioselectivity?, NUCLEOS NUC, 18(4-5), 1999, pp. 867-869
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, th
e lack of enantioselectivity of the enzymes is more frequent than it was be
lieved a few years ago and we suggest that it would depend on chance more t
han on an evolutionary strategy.