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

• Trapping of 8-azido-ADP followed by UV irradiation yielded permanent inactivation and specific labeling of Pgp in plasma membranes [6].

Associations of 8-azidoadenosine diphosphate with other chemical compounds

• 8-azido-ADP, a covalent-binding inhibitor of mitochondrial adenine nucleotide translocation [7].

Gene context of 8-azidoadenosine diphosphate

• 1. Photolabelling of chloroplast ATPase (CF1) with either 8-azido-ATP or 8-azido-ADP leads to inactivation of the ATPase activity [8].
• 4. Upon extrapolation to complete inactivation, 2 mol label, either 8-azido-ATP or 8-azido-ADP can be bound [8].

References