Interaction of beta-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 believed a few years ago and we suggest that it would depend on chance more than on an evolutionary strategy.
Verri
A
A
IGBE, CNR, Pavia, Italy.
Montecucco
A
A
Gosselin
G
G
Boudou
V
V
Spadari
S
S
Imbach
J L
JL
Focher
F
F
D000255:Adenosine Triphosphate / Q000378:metabolism*; D011088:DNA Ligases / Q000378:metabolism*; D019915:DNA Primase / Q000378:metabolism*; D003842:Deoxycytidine Kinase / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D013237:Stereoisomerism; D013379:Substrate Specificity
D000255:Adenosine Triphosphate; D003842:Deoxycytidine Kinase; D019915:DNA Primase; D011088:DNA Ligases