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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2008-4-11
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenine,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Boranes,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphonic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Soman,
http://linkedlifedata.com/resource/pubmed/chemical/adefovir,
http://linkedlifedata.com/resource/pubmed/chemical/adenylate kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/adenylate kinase 2,
http://linkedlifedata.com/resource/pubmed/chemical/pinacolyl methylphosphonic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1525-7770
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pubmed:author |
pubmed-author:AlvaresPP,
pubmed-author:BarralKK,
pubmed-author:CanardBB,
pubmed-author:Deville-BonneDD,
pubmed-author:El-AmriCC,
pubmed-author:GuerreiroCC,
pubmed-author:MulardLL,
pubmed-author:Munier-LehmannHH,
pubmed-author:SchneiderBB,
pubmed-author:TopalisDD,
pubmed-author:VéronMM
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pubmed:issnType |
Print
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pubmed:volume |
27
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
319-31
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pubmed:dateRevised |
2009-9-4
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pubmed:meshHeading |
pubmed-meshheading:18404568-Adenine,
pubmed-meshheading:18404568-Adenosine Triphosphate,
pubmed-meshheading:18404568-Adenylate Kinase,
pubmed-meshheading:18404568-Binding Sites,
pubmed-meshheading:18404568-Boranes,
pubmed-meshheading:18404568-Catalytic Domain,
pubmed-meshheading:18404568-Cloning, Molecular,
pubmed-meshheading:18404568-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:18404568-Humans,
pubmed-meshheading:18404568-Isoenzymes,
pubmed-meshheading:18404568-Kinetics,
pubmed-meshheading:18404568-Models, Molecular,
pubmed-meshheading:18404568-Nucleotides,
pubmed-meshheading:18404568-Phosphonic Acids,
pubmed-meshheading:18404568-Phosphorylation,
pubmed-meshheading:18404568-Recombinant Proteins,
pubmed-meshheading:18404568-Soman
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pubmed:year |
2008
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pubmed:articleTitle |
Acyclic phosphonate nucleotides and human adenylate kinases: impact of a borano group on alpha-P position.
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pubmed:affiliation |
Laboratoire d'Enzymologie, Université Paris, Paris, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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