Acyclic Phosphonate Nucleotides and Human Adenylate Kinases: Impact of a Borano Group on a-P Position

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 a-borano or a-H on PMEA and PMPA were detrimental to the...

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Published inNucleosides, nucleotides & nucleic acids Vol. 27; no. 4; pp. 319 - 331
Main Authors Topalis, D, Alvarez, K, Barral, K, Munier-Lehmann, H, Schneider, B, Veron, M, Guerreiro, C, Mulard, L, El-Amri, C, Canard, B, Deville-Bonne, D
Format Journal Article
LanguageEnglish
Published 01.04.2008
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Summary: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 a-borano or a-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 a-phosphate, resulting in substrate bad positioning.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:1525-7770
1532-2335
DOI:10.1080/15257770801941952