title: 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?
abstract: 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.
authors.affiliation: IGBE, CNR, Pavia, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Verri
authors.forename: A
authors.initials: A
authors.lastname: Montecucco
authors.forename: G
authors.initials: G
authors.lastname: Gosselin
authors.forename: V
authors.initials: V
authors.lastname: Boudou
authors.forename: S
authors.initials: S
authors.lastname: Spadari
authors.forename: J L
authors.initials: JL
authors.lastname: Imbach
authors.forename: F
authors.initials: F
authors.lastname: Focher
mesh_terms: 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
chemical_list: D000255:Adenosine Triphosphate; D003842:Deoxycytidine Kinase; D019915:DNA Primase; D011088:DNA Ligases