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Journal articles
Acyclic phosphonate nucleotides and human adenylate kinases: impact of a borano group on alpha-P position.
D. Topalis
1
K. Alvarez
2
K. Barral
2
Hélène Munier-Lehmann
3
B. Schneider
4
M. Véron
4
C. Guerreiro
3
Laurence A Mulard
3
C. El-Amri
5
B. Canard
2
Dominique Deville-Bonne
1, *
D. Topalis 1
Author
K. Alvarez 2
Author
K. Barral 2
Author
Hélène Munier-Lehmann 3
Author IdHAL : helene-munier-lehmann
1
Enzymologie Moléculaire et Fonctionnelle (France)
- UPMC - Université Pierre et Marie Curie - Paris 6 : UR4 (4 place Jussieu - 75005 Paris - France)
2
AFMB - Architecture et fonction des macromolécules biologiques (Faculté des Sciences de Luminy - Case 932
163, Avenue de Luminy
13288 Marseille Cedex 09 - France)
- INRA - Institut National de la Recherche Agronomique : UMR7257 (France)
- AMU - Aix Marseille Université : UMR7257 (Aix-Marseille Université Jardins du Pharo 58 Boulevard Charles Livon 13284 Marseille cedex 7 - France)
- CNRS - Centre National de la Recherche Scientifique : UMR7257 (France)
3
UCO - Chimie Organique (28 rue du Docteur Roux 75724 Paris Cedex 15 - France)
- Institut Pasteur [Paris] (25-28, rue du docteur Roux, 75724 Paris cedex 15 - France)
- CNRS - Centre National de la Recherche Scientifique : URA2128 (France)
4
Régulation Enzymatique des Activités Cellulaires (28, rue du Dr Roux 75724 Paris cedex 15 - France)
- Institut Pasteur [Paris] (25-28, rue du docteur Roux, 75724 Paris cedex 15 - France)
- CNRS - Centre National de la Recherche Scientifique : URA2185 (France)
5
FRE 2852 - Peptidome de la Peau des Amphibiens (Tour 43, 2 place Jussieu, 75251 Paris Cedex 05 - France)
- UPMC - Université Pierre et Marie Curie - Paris 6 (4 place Jussieu - 75005 Paris - France)
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.
Document type :
Journal articles
Complete list of metadatas
https://hal-pasteur.archives-ouvertes.fr/pasteur-00316017
Contributor : Hélène Munier-Lehmann <>
Submitted on : Tuesday, September 2, 2008 - 12:45:01 PM
Last modification on : Tuesday, March 17, 2020 - 3:32:26 AM
Contributor : Hélène Munier-Lehmann <>
Submitted on : Tuesday, September 2, 2008 - 12:45:01 PM
Last modification on : Tuesday, March 17, 2020 - 3:32:26 AM
Identifiers
- HAL Id : pasteur-00316017, version 1
- DOI : 10.1080/15257770801941952
- PUBMED : 18404568
Collections
PASTEUR | CNRS | UPMC | UNIV-AMU | INRA | SORBONNE-UNIVERSITE | SU-SCIENCES | G2ELAB | UGA | INRAE
Citation
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, Taylor & Francis, 2008, 27 (4), pp.319-31. ⟨10.1080/15257770801941952⟩. ⟨pasteur-00316017⟩
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