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Chemical Compound Review

AC1L3TOJ     [[(2R,3S,4R,5R)-5-(6-amino-8- azido-purin-9...

Synonyms: AR-1H4374, AC1Q6S15, 8-Azido-ADP, UNII-GSN94OF83M, 8-azidoadenosine diphosphate, ...
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High impact information on 8-azidoadenosine diphosphate

  • Trapping of ADP (or 8-azido-ADP) and vanadate (ADP.Vi or 8-azido-ADP.Vi) at the catalytic site, following nucleotide hydrolysis, markedly reduces the affinity of Pgp for its transport substrate [(125)I]iodoarylazidoprazosin ([(125)I]IAAP), resulting in dissociation of the latter [1].
  • Combined mutation of "catalytic carboxylates" in both nucleotide binding domains (NBDs) of P-glycoprotein generates a conformation capable of tight binding of 8-azido-ADP (Sauna, Z. E., Müller, M., Peng, X. H., and Ambudkar, S. V. (2002) Biochemistry 41, 13989-14000) [2].
  • When disk membranes or membranes from co-transfected cells were photoaffinity labeled with 8-azido-ATP and 8-azido-ADP, only the NBD2 in the C-half bound and trapped the nucleotide [3].
  • This binding is followed by minimal Mg(2+)-dependent hydrolysis and retention of the hydrolysis product, 8-azido-ADP, but not as a vanadate stabilized post-hydrolysis transition state complex [4].
  • Interaction of the photoaffinity label 8-azido-ADP with glutamate dehydrogenase [5].

Anatomical context of 8-azidoadenosine diphosphate


Associations of 8-azidoadenosine diphosphate with other chemical compounds


Gene context of 8-azidoadenosine diphosphate


  1. Allosteric Modulation Bypasses the Requirement for ATP Hydrolysis in Regenerating Low Affinity Transition State Conformation of Human P-glycoprotein. Maki, N., Moitra, K., Ghosh, P., Dey, S. J. Biol. Chem. (2006) [Pubmed]
  2. Combined mutation of catalytic glutamate residues in the two nucleotide binding domains of P-glycoprotein generates a conformation that binds ATP and ADP tightly. Tombline, G., Bartholomew, L.A., Urbatsch, I.L., Senior, A.E. J. Biol. Chem. (2004) [Pubmed]
  3. Functional interaction between the two halves of the photoreceptor-specific ATP binding cassette protein ABCR (ABCA4). Evidence for a non-exchangeable ADP in the first nucleotide binding domain. Ahn, J., Beharry, S., Molday, L.L., Molday, R.S. J. Biol. Chem. (2003) [Pubmed]
  4. The First Nucleotide Binding Domain of Cystic Fibrosis Transmembrane Conductance Regulator Is a Site of Stable Nucleotide Interaction, whereas the Second Is a Site of Rapid Turnover. Aleksandrov, L., Aleksandrov, A.A., Chang, X.B., Riordan, J.R. J. Biol. Chem. (2002) [Pubmed]
  5. Interaction of the photoaffinity label 8-azido-ADP with glutamate dehydrogenase. Koberstein, R., Cobianchi, L., Sund, H. FEBS Lett. (1976) [Pubmed]
  6. Inhibition of P-glycoprotein ATPase activity by beryllium fluoride. Sankaran, B., Bhagat, S., Senior, A.E. Biochemistry (1997) [Pubmed]
  7. 8-azido-ADP, a covalent-binding inhibitor of mitochondrial adenine nucleotide translocation. SchHafer, G., Schrader, E., Rowohl-Quisthoudt, G., Penades, S., Rimpler, M. FEBS Lett. (1976) [Pubmed]
  8. Photolabelling with 8-azido-adenine nucleotides of adenine nucleotide-binding sites in isolated spinach chloroplast ATPase (CF1). Wagenvoord, R.J., Verschoor, G.J., Kemp, A. Biochim. Biophys. Acta (1981) [Pubmed]
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