2. Academic Validation
  3. Probing binding requirements of NAD kinase with modified substrate (NAD) analogues

Probing binding requirements of NAD kinase with modified substrate (NAD) analogues

  • Bioorg Med Chem Lett. 2007 Mar 15;17(6):1512-5. doi: 10.1016/j.bmcl.2007.01.012.
Laurent Bonnac 1,  Liqiang Chen,  Rashmi Pathak,  Guangyao Gao,  Qian Ming,  Eric Bennett,  Krzysztof Felczak,  Martin Kullberg,  Steven E Patterson,  Francesca Mazzola,  Giulio Magni,  Krzysztof W Pankiewicz
Affiliations

Affiliation

  • 1 Center for Drug Design, University of Minnesota, Minneapolis, MN 55455, USA.
PMID: 17258457 DOI: 10.1016/j.bmcl.2007.01.012
Abstract

Synthesis of novel NAD(+) analogues that cannot be phosphorylated by NAD kinase is reported. In these analogues the C2' hydroxyl group of the adenosine moiety was replaced by fluorine in the ribo or arabino configuration (1 and 2, respectively) or was inverted into arabino configuration to give compound 3. Compounds 1 and 2 showed inhibition of human NAD kinase, whereas analogue 3 inhibited both the human and Mycobacterium tuberculosis NAD kinase. An uncharged benzamide adenine dinucleotide (BAD) was found to be the most potent competitive inhibitor (K(i)=90 microM) of the human Enzyme reported so far.

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