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Chemical Compound Review:

AC1LD8Z3 [[[(2R,3S,4R,5R)-5-(6-amino- 8-azido-purin...

Synonyms: 117145-99-0, 8-Azido-[alpha-32P]ATP, 8-Azidoadenosine-[alpha-32P]triphosphate, 8-Azidoadenosine 5'-[alpha-32P]triphosphate

Tanaka, A.R. et al., Kudlicki, W. et al., LeBel, D. et al., Howell, L.D. et al., Szabó, K. et al., et al.

Ueda, Komine, Matsuo, Seino, Amachi,

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Disease relevance of adenosine, 8-azido-, 5'-(tetrahydrogen [alpha-32P]triphosphate)

We have covalently modified the recA protein from Escherichia coli with the photoaffinity ATP analog 8-azido-[alpha-32P]ATP (N3-ATP) [1].

High impact information on adenosine, 8-azido-, 5'-(tetrahydrogen [alpha-32P]triphosphate)

The amino acid sequence of Ste6 predicts two ATP-binding folds; correspondingly, Ste6 was photoaffinity-labeled specifically with 8-azido-[alpha-32P]ATP [2].
Here, we report that MgATP and MgADP, but not the Mg salt of gamma-thio-ATP, stabilize the binding of prebound 8-azido-[alpha-32P]ATP to SUR1 [3].
Incubation of these membranes with 8-azido-[alpha-32P]ATP and subsequent irradiation with UV light resulted in covalent labeling of a major band of Mr 43,000 [4].
PMP70 was photoaffinity-labeled at similar efficiencies with 8-azido-[alpha-32P]ATP and 8-azido-[gamma-32P]ATP when peroxisomes were incubated with these nucleotides at 37 degrees C in the absence Mg2+ and exposed to UV light without removing unbound nucleotides [5].
However, none of the mAbs inhibited photolabeling of intact MRP with 8-azido-[alpha-32P]ATP [6].

Biological context of adenosine, 8-azido-, 5'-(tetrahydrogen [alpha-32P]triphosphate)

A Mr 95,000 peptide, detectable only by photoaffinity labeling with 8-azido-[alpha 32P]ATP, is shown to be distinct from the Mr 100,000 phosphopeptide and appears to be the catalytic subunit of the eIF-2 alpha kinase [7].
Photoaffinity labeling using 8-azido-[alpha-32P]ATP or [y-32P]ATP confirms the presence of ATP binding sites [8].
Photoaffinity labeling experiments with 8-azido-[alpha-32P]ATP showed that ATP binding at NBD2 is reduced by the suppressor mutation in TM12 [9].
When fusion proteins were photolabelled with 8-azido-[alpha-32P]ATP, PKA phosphorylation increased the apparent k(d) for nucleotide binding and it caused binding to become co-operative [10].

Anatomical context of adenosine, 8-azido-, 5'-(tetrahydrogen [alpha-32P]triphosphate)

Here we describe that human CFTR expressed in insect (Sf9) cell membranes shows specific, Mg2+-dependent nucleotide occlusion, detected by covalent labeling with 8-azido-[alpha-32P]ATP [11].
Photolabeling of coated vesicles with 8-azido-[alpha-32P]ATP results in specific labeling of only the Mr 53 000 and Mr 51 000 peptides [12].
8-Azido-[alpha-32P]ATP (8-N3-ATP) was used as a photoaffinity label for ATP binding sites in the subcellular fractions of rabbit peritoneal neutrophils [13].
Under these same conditions, 8-azido-[alpha-32P]ATP reacted with a number of polypeptides of the intact lysosome and lysosomal membranes [14].

Associations of adenosine, 8-azido-, 5'-(tetrahydrogen [alpha-32P]triphosphate) with other chemical compounds

Further evidence that the p68 kinase can be activated by heparin was provided by photoaffinity labeling with 8-azido-[alpha-32P]ATP [15].

Gene context of adenosine, 8-azido-, 5'-(tetrahydrogen [alpha-32P]triphosphate)

Interestingly, excess unlabeled ATP could enhance photoaffinity labeling of 8-azido-[alpha-32P]ATP to Vps33p, suggesting cooperative binding, which was not observed with excess GTP [16].
The azido photoprobe, 8-azido-[alpha-32P]ATP, has been used to identify the ATP binding domain of the recombinant human 40-kDa 2-5A synthetase [17].
The photolabeling of P-glycoprotein with 8-azido-[alpha-32P]ATP was inhibited by C219, suggesting that the inhibition of ATP binding by C219 reduced the activity [18].
Identification of the catalytic subunit of the ATP diphosphohydrolase by photoaffinity labeling of high-affinity ATP-binding sites of pancreatic zymogen granule membranes with 8-azido-[alpha-32P]ATP [19].
Rough ER proteins of apparent molecular masses 141, 111, 100, 84, 69, 55 and 47 kDa were detected following photoaffinity-labelling with 8-azido-[alpha-32P]ATP [20].

References

Covalent modification of the recA protein from Escherichia coli with the photoaffinity label 8-azidoadenosine 5'-triphosphate. Knight, K.L., McEntee, K. J. Biol. Chem. (1985) [Pubmed]
The a-factor transporter (STE6 gene product) and cell polarity in the yeast Saccharomyces cerevisiae. Kuchler, K., Dohlman, H.G., Thorner, J. J. Cell Biol. (1993) [Pubmed]
Cooperative binding of ATP and MgADP in the sulfonylurea receptor is modulated by glibenclamide. Ueda, K., Komine, J., Matsuo, M., Seino, S., Amachi, T. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
Identification of a molecular weight 43,000 protein kinase in acetylcholine receptor-enriched membranes. Gordon, A.S., Milfay, D., Diamond, I. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
ATP binding/hydrolysis by and phosphorylation of peroxisomal ATP-binding cassette proteins PMP70 (ABCD3) and adrenoleukodystrophy protein (ABCD1). Tanaka, A.R., Tanabe, K., Morita, M., Kurisu, M., Kasiwayama, Y., Matsuo, M., Kioka, N., Amachi, T., Imanaka, T., Ueda, K. J. Biol. Chem. (2002) [Pubmed]
Monoclonal antibodies that inhibit the transport function of the 190-kDa multidrug resistance protein, MRP. Localization of their epitopes to the nucleotide-binding domains of the protein. Hipfner, D.R., Mao, Q., Qiu, W., Leslie, E.M., Gao, M., Deeley, R.G., Cole, S.P. J. Biol. Chem. (1999) [Pubmed]
Identification of spectrin-related peptides associated with the reticulocyte heme-controlled alpha subunit of eukaryotic translational initiation factor 2 kinase and of Mr 95,000 peptide that appears to be the catalytic subunit. Kudlicki, W., Fullilove, S., Read, R., Kramer, G., Hardesty, B. J. Biol. Chem. (1987) [Pubmed]
Partial characterization of a new nucleotide binding glycoprotein of hepatocyte plasma membrane. Kreisel, W., Spamer, C., Heilmann, C. Biochem. Pharmacol. (1996) [Pubmed]
Functional asymmetry of the two nucleotide binding domains in the ABC transporter Ste6. Proff, C., Kölling, R. Mol. Gen. Genet. (2001) [Pubmed]
Protein kinase A regulates ATP hydrolysis and dimerization by a CFTR (cystic fibrosis transmembrane conductance regulator) domain. Howell, L.D., Borchardt, R., Kole, J., Kaz, A.M., Randak, C., Cohn, J.A. Biochem. J. (2004) [Pubmed]
Nucleotide occlusion in the human cystic fibrosis transmembrane conductance regulator. Different patterns in the two nucleotide binding domains. Szabó, K., Szakács, G., Hegeds, T., Sarkadi, B. J. Biol. Chem. (1999) [Pubmed]
Identification of a protein kinase as an intrinsic component of rat liver coated vesicles. Campbell, C., Squicciarini, J., Shia, M., Pilch, P.F., Fine, R.E. Biochemistry (1984) [Pubmed]
The photoaffinity probe 8-N3[alpha-32P]ATP labels the ATP-binding sites of rabbit neutrophil and skeletal muscle actin. Huang, C.K., Hill, J.M., Bormann, B.J., Mackin, W.M., Becker, E.L. FEBS Lett. (1983) [Pubmed]
The lysosomal H+ pump: 8-azido-ATP inhibition and the role of chloride in H+ transport. Cuppoletti, J., Aures-Fischer, D., Sachs, G. Biochim. Biophys. Acta (1987) [Pubmed]
The double-stranded RNA-dependent protein kinase is also activated by heparin. Hovanessian, A.G., Galabru, J. Eur. J. Biochem. (1987) [Pubmed]
The vesicle transport protein Vps33p is an ATP-binding protein that localizes to the cytosol in an energy-dependent manner. Gerhardt, B., Kordas, T.J., Thompson, C.M., Patel, P., Vida, T. J. Biol. Chem. (1998) [Pubmed]
Identification of the ATP binding domain of recombinant human 40-kDa 2',5'-oligoadenylate synthetase by photoaffinity labeling with 8-azido-[alpha-32P]ATP. Kon, N., Suhadolnik, R.J. J. Biol. Chem. (1996) [Pubmed]
Functional modulation of ATPase of P-glycoprotein by C219, a monoclonal antibody against P-glycoprotein. Kokubu, N., Cohen, D., Watanabe, T. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
Identification of the catalytic subunit of the ATP diphosphohydrolase by photoaffinity labeling of high-affinity ATP-binding sites of pancreatic zymogen granule membranes with 8-azido-[alpha-32P]ATP. LeBel, D., Beattie, M. Biochem. Cell Biol. (1986) [Pubmed]
Photoaffinity labelling of the ATP-binding sites of two Ca2+,Mg-ATPase isoforms in pancreatic endoplasmic reticulum. Webb, R., Dormer, R.L. Biochim. Biophys. Acta (1995) [Pubmed]

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