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

Laurent Bonnac, Liqiang Chen, Rashmi Pathak, Guangyao Gao, Qian Ming, Eric Bennett, Krzysztof Felczak, Martin Kullberg, Steven E. Patterson, Francesca Mazzola, Giulio Magni, Krzysztof W. Pankiewicz

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


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 (Ki = 90 μM) of the human enzyme reported so far.

Original languageEnglish (US)
Pages (from-to)1512-1515
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Issue number6
StatePublished - Mar 15 2007

Bibliographical note

Funding Information:
These studies were funded by the Center for Drug Design, University of Minnesota.


  • Benzamide adenine dinucleotide (BAD)
  • M. tuberculosis
  • NAD analogues
  • NAD kinase


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