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Acyclic phosphonate nucleotides and human adenylate kinases: impact of a borano group on alpha-P position.

Abstract : Adenylate kinases are involved in the activation of antiviral drugs such as the acyclic phosphonates analogs PMEA and (R)PMPA. We examine the in vitro phosphorylation of PMEA and PMPA bearing a borano- or a H- group on the phosphorus atom. The alpha-borano or alpha-H on PMEA and PMPA were detrimental to the activity of recombinant human AMP kinases 1 and 2. Docking PMEA to the active site of AMP kinase 1 indicated that the borano group may prevent two conserved critical Arg interactions with the alpha-phosphate, resulting in substrate bad positioning.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-00316017
Contributor : Hélène Munier-Lehmann Connect in order to contact the contributor
Submitted on : Tuesday, September 2, 2008 - 12:45:01 PM
Last modification on : Thursday, April 7, 2022 - 10:10:12 AM

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D. Topalis, K. Alvarez, K. Barral, Hélène Munier-Lehmann, B. Schneider, et al.. Acyclic phosphonate nucleotides and human adenylate kinases: impact of a borano group on alpha-P position.. Nucleosides, Nucleotides and Nucleic Acids, 2008, 27 (4), pp.319-31. ⟨10.1080/15257770801941952⟩. ⟨pasteur-00316017⟩

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