2'/3'-O-(N-Methyl-anthraniloyl)-adenosine-5'-diphosphate, Triethylammonium salt
For research use only!
Shipping: shipped on gel packs
Storage Conditions: store at -20 °C
Short term exposure (up to 1 week cumulative) to ambient temperature possible.
Shelf Life: 12 months after date of delivery
Molecular Formula: C18H22N6O11P2 (free acid)
Molecular Weight: 560.35 g/mol (free acid)
Exact Mass: 560.08 g/mol (free acid)
Purity: ≥ 95 % (HPLC)
Form: solution in water
Color: colorless to slightly yellow
Concentration: 10 mM - 11 mM
pH: 7.5 ±0.5
Spectroscopic Properties: λmax 255/355 nm, ε 23.3/5.8 L mmol-1 cm-1 (Tris-HCl pH 7.5), λexc 355 nm, λem 448 nm
Dissociation kinetic proteinkinase A
FRET: kinesin, myosin[5, 1]
Conformational dynamic: DnaC-protein
Kinesin head domains
BIOZ Product Citations:
Please click the arrow on the right to expand the citation list. Click publication title for the full text.
 Robertson et al. (2005) Structural rearrangements in the active site of smooth muscle myosin. Biophysical J. 89:1882.
 Fak et al. (2004) Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state. Biochemistry 43:7307.
 Ni et al. (2000) Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives. Protein Science 9:1818.
 Hackney et al. (2009) Half-site inhibition of dimeric kinesin head domains by monomeric tail domains. Biochemistry 48:3448.
 Sun et al. (2006) Dynamics of the upper 50-kDa domain of myosin V examined with fluorescence resonance energy transfer. J. Biol. Chem. 281:5711.
 Galletto et al. (2005) The nucleotide-binding site ot the Escherichia coli DnaC protein: Molecular topography of DnaC protein-nucleotide cofactor complex. Cell Biochem. and Biophys. 43:331.
Pinto et al. (2011) Structure-activity relationships for the interactions of 2'- and 3'- (O)- (N-methyl)anthraniloyl-substituted purine and pyrimidine nucleotides with mammalian adenylyl cyclases. Molecular Pharmacology 82 (4):358.
Chen et al. (2009) ADP but Not Pi Dissociation Contributes to Rate Limitation for Escherichia coli Rho*. J. Biol. Chem. 284 (49):33773.
Taha et al. (2009) Molecular Analysis of the Interaction of Anthrax Adenylyl Cyclase Toxin, Edema Factor, with 2' (3')-O- (N- (methyl)anthraniloyl)-Substituted Purine and Pyrimidine Nucleotides. Molecular Pharmacology 75 (3):693.
Del Toro Duany et al. (2008) The reverse gyrase helicase-like domain is a nucleotide-dependent switch that is attenuated by the topoisomerase domain. Nucleic Acids Research 36 (18):5882.
Kainov et al. (2008) Structural Basis of Mechanochemical Coupling in a Hexameric Molecular Motor. The Journal of biological chemistry 283 (6):3607.
Bujalowski et al. (2000) Kinetic mechanism of nucleotide cofactor binding to Escherichia coli replicative helicase DnaB protein. stopped-flow kinetic studies using fluorescent, ribose-, and base-modified nucleotide analogues. Biochemistry 39:2106.
Rice et al. (1999) A structural change in the kinesin motor protein that drives motility. Nature 402:778.
Cheng et al. (1998) Interaction of mant-adenosine nucleotides and magnesium with kinesin. Biochemistry 37:5288.
Bauer et al. (1997) X-ray crystal structure and solution fluorescence characterization of Mg-2' (3')-O- (N-methylanthraniloyl) nucleotides bound to the Dictyostelium discoideum myosin motor domain. J. Mol. Biol. 274:394.
Bujalowski et al. (1994) Structural characteristics of the nucleotide-binding site of Escherichia coli primary replicative helicase DnaB protein. Studies with ribose and base-modified fluorescent nucleotide analogs. Biochemistry 33:4682.
Moore et al. (1994) Kinetic mechanism of adenine nucleotide binding to and hydrolysis by the Escherichia coli Rep monomer. 1. Use of fluorescent nucleotide analogues. Biochemistry 33:14550.
Hiratsuka (1983) New ribose-modified fluorescent analogs of adenine and guanine nucleotides available as substrates for various enzymes. Biochim. Biophys. Acta 742:496.