Nucleotide Analogs - Jena Bioscience

Nucleotide Analogs
60
Adenosine Nucleotides
NPE-caged-ATP
Adenosine-5’-triphosphate, P 3 -(1-(2-nitrophenyl)ethyl)-ester,
Triethylammonium salt
Cat. No. Amount (Units) Price (€)
NU-301S 150 75,--
NU-301L 750 300,--
Molecular Formula: C 18 H 20 N 6 O 15 P 3 (Anion)
Molecular Weight: 653.30 (Anion)
NO2 CH3 O
O
O
P
O O
O
O O
P O P O
3 (CH3CH2)3NH
OH
O
OH
N
N
NH 2
Selected references:
Zscherp et al. (2001) Reaction-induced infrared difference
spectroscopy for the study of protein reaction mechanisms.
Biochemistry 40:1875.
Scheirlinckx et al. (2001) Monitoring of secondary and tertiary
structure changes in the gastric H + /K + -ATPase by infrared spectroscopy
Eur. J. Biochem. 268 (13):3644.
Barth et al. (2000) Substrate binding and enzyme function
investigated by infrared spectroscopy. FEBS Lett. 477:151.
Hess (1999) Light-Activated (Caged) Biological Ligands. Encyclopedia
of Molecular Biology, Vol. 3, T.E. Creighton (Ed.), pp.
1385-1391.
Broustovetsky et al. (1997) Biochemical and physical parameters
of the electrical currents measured with the ADP/ATP
carrier by photolysis of caged ADP and ATP. Biochemistry 36:
13865.
Higuchi et al. (1997) Kinetics of force generation by single
kinesin molecules activated by laser photolysis of caged ATP.
P. Natl. Acad. Sci. USA 94:4395.
Emoto et al. (1995) Tension relaxation induced by pulse photolysis
of caged ATP in partially crosslinked fi bers from rabbit
psoas muscle.
P. Natl. Acad. Sci. USA 92:1461.
Barth et al. (1995) Photochemical Release of ATP from “Caged
ATP” Studied by Time-Resolved Infrared Spectroscopy. J. Am.
Chem. Soc. 117:10311.
Hyman et al. (1992) Microtubule-motor activity of a yeast centromere-binding
protein complex. Nature 359:533.
Fajer et al. (1990) Myosin heads have a broad orientational
distribution during isometric muscle contraction: time-resolved
EPR studies using caged ATP. P. Natl. Acad. Sci. USA 87:
5538.
Walker et al. (1988) Photolabile 1-(2-Nitrophenyl)ethyl Phosphate
Esters of Adenine Nucleotide Analogues. Synthesis and
Mechanism of Photolysis. J. Am. Chem. Soc. 110:7170.
Goldman et al. (1982) Relaxation of muscle-fi bers by photolysis
of caged ATP. Nature 300:701.
DMB-caged-ATP
Adenosine-5’-triphosphate, P 3 -(1-(3’,5’dimethoxyphenyl)-
2-oxo-2-phenyl-ethyl)-ester,
Triethylammonium salt
Cat. No. Amount (Units) Price (€)
NU-309S 10 75,--
NU-309L 50 300,--
Molecular Formula: C 26 H 27 N 5 O 16 P 3 (Anion)
Molecular Weight: 758.44 (Anion)
H3CO
OCH3
O
O
O
O
O
O
P
O
O O
P O P O
3 (CH3CH2)3NH
OH
O
OH
N
N
N
NH 2
N
N
N
Selected references:
Apell et al. (1998) Partial reactions of the Na,K-ATPase: kinetic
analysis and transport properties. Acta Physiol. Scand. 163:
235.
Sokolov et al. (1998) Fast transient currents in Na,K-ATPase
induced by ATP concentration jumps from the P-3-[1-(3’,5’dimethoxyphenyl)-2-phenyl-2-oxo]ethyl
ester of ATP. Biophys.
J. 74 (5):2285.
Sokolov et al. (1997) Fast transient currents in the Na,K-
ATPase induced by ATP concentration jump experiments from
DMB-caged ATP. Biophys. J. 72 (2):242.
Thirlwell et al. (1995) Inhibition of unloaded shortening velocity
in permeabilized muscle-fi bers by caged-ATP compounds. J.
Muscle Res. Cell M. 16 (2):131.
Thirlwell et al. (1994) Kinetics of relaxation from rigor of permeabilized
fast-twitch skeletal fi bers from the rabbit using a novel
caged-ATP and apyrase. Biophys. J. 67 (6):2436.
Corrie et al. (1992) Synthetic, mechanistic and photochemical
studies of phosphate-esters of substituted benzoins. J. Chem.
Soc. Perk. T. 1 18: 2409.
Corrie et al. (1992) The development and application of photosensitive
caged compounds to aid time-resolved structure
determination of macromolecules. Philos. T. Roy. Soc. A 340
(1657):233.
NPE-caged-AppNHp
(NPE-caged-AMPPNP)
Adenosine-5’-[(β,γ)-imido]triphosphate, P 3 -(1-(2nitrophenyl)-ethyl)-ester,
Triethylammonium salt
Cat. No. Amount (Units) Price (€)
NU-305S 100 75,--
NU-305L 500 300,--
Molecular Formula: C H N O P (Anion)
18 21 7 14 3
Molecular Weight: 652.32 (Anion)
NO2 CH3 O
O
O
P
O O
NH
O O
P O P O
3 (CH 3CH 2) 3NH
OH
O
OH
Guanosine Nucleotides
NPE-caged-GTP
Guanosine-5’-triphosphate, P 3 -(1-(2-nitrophenyl)ethyl)-ester,
Triethylammonium salt
Cat. No. Amount (Units) Price (€)
NU-302S 100 75,--
NU-302L 500 300,--
Molecular Formula: C 18 H 20 N 6 O 16 P 3 (Anion)
Molecular Weight: 669.30 (Anion)
NO2 CH3 O
O
O
P
O O
O
O O
P O P O
3 (CH 3CH 2) 3NH
OH
O
OH
N
N
N
N
O
N
NH
NH 2
N
NH 2
Selected references:
Allin et al. (2001) Monitoring the GAP catalyzed H-Ras GTPase
reaction at atomic resolution in real time. P. Natl. Acad. Sci. USA
98 (14):7754.
Allin et al. (2001) Ras catalyzes CTP hydrolysis by shifting
negative charges from γ- to β-phosphate as revealed by timeresolved
FTIR difference spectroscopy. Biochemistry-US 40
(10):3037.
Scheidig et al. (1999) The pre-hydrolysis state of p21(ras) in
complex with GTP: new insights into the role of water molecules
N
http://www.jenabioscience.com
in the GTP hydrolysis reaction of ras-like proteins. Struct. Fold.
Des. 7 (11):1311.
Gerwert (1999) Molecular reaction mechanisms of proteins
monitored by time-resolved FTIR-spectroscopy. Biol. Chem.
380 (7-8):931.
Cepus et al. (1998) Time-resolved FTIR studies of the GTPase
reaction of H-ras p21 reveal a key role for the β-phosphate.
Biochemistry 37 (28):10263.
Wagner et al. (1995) Interaction of guanosine nucleotides
and their analogs with elongation-factor tu from thermusthermophilus.
Biochemistry 34 (39):12535.
Scheidig et al. (1995) X-ray crystal-structure analysis of
the catalytic domain of the oncogene product p21(H-ras)
complexed with caged GTP and mant-dGppNHp. J. Mol. Biol.
253 (1):132.
Scheidig et al. (1994) Crystallographic studies on p21(H-Ras)
using the synchrotron laue method - improvement of crystal
quality and monitoring of the GTPase reaction at different time
points. Acta Cryst. D 50:512.
Scheidig et al. (1992) Time-resolved crystallography on H-Ras
p21. Philos. T. Roy. Soc. A 340 (1657):263.
Reshetnikova et al. (1992) Crystals of intact elongation factor-
Tu from thermus-thermophilus diffracting to 1.45-angstrom
resolution. J. Cryst. Growth 122 (1-4):360.
Limmer et al. (1992) Nucleotide binding and gtp hydrolysis by
elongation-factor tu from thermus-thermophilus as monitored
by proton NMR. Biochemistry 31 (11):2970.
Marx et al. (1990) Microtubule assembly and oscillations
induced by fl ash-photolysis of caged-GTP. Eur. Biophys. J.
19 (1):1.
Schlichting et al. (1989) Biochemical and crystallographic
characterization of a complex of c-ha-ras p21 and caged gtp
with fl ash-photolysis - (time-resolved structure). P. Natl. Acad.
Sci. USA 86 (20):7687.
NPE-caged-mant-dGTP
3’-O-(N-Methyl-anthraniloyl)-2’-deoxy-guanosine-
5’-triphosphate, P 3 -(1-(2-nitrophenyl)-ethyl)-ester,
Triethylammonium salt
Cat. No. Amount (Units) Price (€)
NU-303S 10 75,--
NU-303L 50 300,--
Molecular Formula: C 26 H 27 N 7 O 16 P 3 (Anion)
Molecular Weight: 786.45 (Anion)
NO2 CH3 O
O
O
P
O O
O
O O
P O P O
3 (CH3CH2)3NH
NPE-caged-GpCpp
(NPE-caged-GMPCPP)
O
O
O
NH
CH3
N
N
O
N
NH
NH2
Guanosine-5’-[(α,β)-methyleno]triphosphate, P 3 -(1-(2nitrophenyl)-ethyl)-ester,
Triethylammonium salt
Cat. No. Amount (Units) Price (€)
NU-306S 10 75,--
NU-306L 50 300,--
Molecular Formula: C 19 H 22 N 6 O 15 P 3 (Anion)
Molecular Weight: 667.33 (Anion)
NO2 CH3 O
O
O
P
O O
O
O O
P P
CH2 O
3 (CH 3CH 2) 3NH
OH
O
OH
N
N
O
N
NH
NH 2