Interaction of β-l-adenosine-s'-triphosphate (l-atp) with human deoxycytidine kinase, human dna primase and t4 dna ligase: does the chance direct enzymatic enanhoselecnvtty?

Article abstract of DOI:10.1080/15257779908041585

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. Copyright 1999 by Marcel Dekker, Inc.

Full text of DOI:10.1080/15257779908041585

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Nucleosides and Nucleotides
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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?
A. Verri a , A. Montecucco a , G. Gosselin b , V. Boudou b , S. Spadari
a , J-L. Imbach b & F. Focher a
a IGBE, CNR , Via Abbiategrasso 207, I-27100, PAVIA, Italy
b Laboratoire de Chimie Bioorganique UMR CNRS-USTL 5625 ,
Université Montpellier II , 34095, Montpellier cedex 5, France
Published online: 04 Oct 2006.
To cite this article: A. Verri , A. Montecucco , G. Gosselin , V. Boudou , S. Spadari , J-L. Imbach & F.
Focher (1999) 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?,
Nucleosides and Nucleotides, 18:4-5, 867-869, DOI: 10.1080/15257779908041585
To link to this article: http://dx.doi.org/10.1080/15257779908041585
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