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CAS No. : | 58-64-0 | MDL No. : | MFCD00066473 |
Formula : | C10H15N5O10P2 | Boiling Point : | - |
Linear Structure Formula : | - | InChI Key : | XTWYTFMLZFPYCI-KQYNXXCUSA-N |
M.W : | 427.20 | Pubchem ID : | 6022 |
Synonyms : |
Adenosine diphosphate;ADP;Ado-5'-P-P;5′-ADP;adenosine pyrophosphate
|
Num. heavy atoms : | 27 |
Num. arom. heavy atoms : | 9 |
Fraction Csp3 : | 0.5 |
Num. rotatable bonds : | 6 |
Num. H-bond acceptors : | 13.0 |
Num. H-bond donors : | 6.0 |
Molar Refractivity : | 84.49 |
TPSA : | 252.22 Ų |
GI absorption : | Low |
BBB permeant : | No |
P-gp substrate : | No |
CYP1A2 inhibitor : | No |
CYP2C19 inhibitor : | No |
CYP2C9 inhibitor : | No |
CYP2D6 inhibitor : | No |
CYP3A4 inhibitor : | No |
Log Kp (skin permeation) : | -12.19 cm/s |
Log Po/w (iLOGP) : | -0.53 |
Log Po/w (XLOGP3) : | -4.62 |
Log Po/w (WLOGP) : | -2.06 |
Log Po/w (MLOGP) : | -4.15 |
Log Po/w (SILICOS-IT) : | -4.63 |
Consensus Log Po/w : | -3.2 |
Lipinski : | 2.0 |
Ghose : | None |
Veber : | 1.0 |
Egan : | 1.0 |
Muegge : | 4.0 |
Bioavailability Score : | 0.11 |
Log S (ESOL) : | 0.57 |
Solubility : | 1590.0 mg/ml ; 3.73 mol/l |
Class : | Highly soluble |
Log S (Ali) : | -0.05 |
Solubility : | 378.0 mg/ml ; 0.884 mol/l |
Class : | Very soluble |
Log S (SILICOS-IT) : | 2.15 |
Solubility : | 59800.0 mg/ml ; 140.0 mol/l |
Class : | Soluble |
PAINS : | 0.0 alert |
Brenk : | 1.0 alert |
Leadlikeness : | 1.0 |
Synthetic accessibility : | 4.62 |
Signal Word: | Warning | Class: | N/A |
Precautionary Statements: | P280-P305+P351+P338 | UN#: | N/A |
Hazard Statements: | H302 | Packing Group: | N/A |
GHS Pictogram: |
* All experimental methods are cited from the reference, please refer to the original source for details. We do not guarantee the accuracy of the content in the reference.
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With (E)-N-(4-(1-benzoylpiperidin-4-yl)butyl)-3-(pyridin-3-yl)acrylamide; tris(3-hydroxypropyl)phosphine; nicotinamide phosphoribosyltransferase; water; tris hydrochloride; magnesium chloride; at 37℃;pH 7.5;Enzymatic reaction;Kinetics; | For the NTPase assays, NAMPT or NAMPT-H247A was incubated at 37 C with an NTP in TMT buffer (50 mM Tris-HCl, 10 mM MgC12, 1 mM THP, pH 7.5). The routinely-used NTP concentration was 2 mM. However, for the kinetic analysis <strong>[56-65-5]ATP</strong> and GTP hydrolysis, the NTP concentration ranged from 0.25 mM to 4 mM. Other agents (FK-866, CHS-828, GNI-50, PNP, NMN) were included where indicated. At the indicated times, an aliquot of the sample was quenched by the addition of an equal volume of 1 M perchloric acid (PCA). Samples were stored at -80 C until processed for LC/MS/MS. The values for Vmax and Km (<strong>[56-65-5]ATP</strong> and GTP hydrolysis) were deduced using the on-line Michaelis-Menten kinetics tool at (0160) http://www.graphpad.com/quickcalcs/ttestl/?Format=SEM For the NMN production assay, NAMPT (20 nM) was incubated in the presence of NAM (10 muMu), PRPP (50 muMu) in TMT buffer. Where indicated, NTPs (2 mM) were also included. NMN was assayed using a chemical method which converts NMN into a fluorescent derivative. Briefly, an aliquot (37.5 mu) of the NMN- containing sample was sequentially mixed with 15 mu of 20% acetophenone (in DMSO) and 15 mu of 2M KOH. The mixture was placed on ice for approximately 10 min. Next, 67.5 mu of 100% formic acid was added to each sample, vortexed, and then incubated at 37 C for 20 min. Samples (100 mu) were transferred to a 96-well opaque bottom plate and fluorescence (Ex/Em = 382/445 nm) was measured using a SpectraMax M5 plate reader (Molecular Devices, Sunnyvale, CA). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With nucleoside triphosphate diphosphohydrolase from Legionella pneumophila; In aq. buffer; at 37 - 99℃; for 0.25h;Enzymatic reaction;Kinetics; | The reaction mixture for the Lp1NTPDase inhibition assay contained 50 lL ADP (final concentration 500 lM) dissolved in assay buffer, 10 lL of test compound, and 30 lL of enzyme buffer in a reaction tube. The enzymatic reaction was initiated by adding 10 lL of enzyme solution to each test tube, carried out at 37Cfor 10 min and stopped by heating at 99C for 5 min. Then 100 lL of internal standard UMP (40 lM or 50lM) was added, 100 lL of the resulting solution was transferred to a CE vial and subjected to the CE. | |
With SmNPP5;Enzymatic reaction; | SmNPP5 has additional promiscuity and has been shown to cleave substrates in addition to ADP. As a non-limiting example, SmNPP5 has been shown to cleave Ap3A (diadenosine triphosphate) into AMP and Pi (see e.g., FIG. 9A-FIG. 9C). As another non limiting example, SmNPP5 has been shown to cleave Ap4A (diadenosine tetraphosphate) into AMP and PPi (see e.g., FIG. 10A-FIG. 10C). Ap3A and Ap4A are both canonical ATPase inhibitors. Without wishing to be bound by theory, it is proposed that cleavage of Ap3 A or Ap4A by SmNPP5 can have an effect on coagulation, such as an anti-coagulation effect. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With calcium chloride; In water; | ADP was dissolved at 100 mg/ml in DW and a half-molar amount of CaC12 dissolved at 100 mg/ml slowly dripped into the solution. The resultant ADP-Ca-ADP chelate was lyophilized. |
Yield | Reaction Conditions | Operation in experiment |
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20.6% | Example 1: tBoc-LysAMP-AMC Synthesis and Characterization tBoc-Lys AMP-AMC was made as a modification of the adenosine 5'phosphoramidate synthesis method of Fu et al. (Chemistry Communications 2003 33:134-135). Under an argon atmosphere at room temperature, 0.25 mmol of tBoc-Lys- AMC (Bachem Biosciences Inc., King of Prussia, PA) and 0.12 mmol ADP (SigmaChemical Co., St. Louis, MO) were dissolved in 2 ml pyridine plus 0.6 ml trimethylsilyl chloride, added dropwise, and the resulting mixture was stirred for 2 days. The mixture was evaporated and 1 ml of 2M aqueous ammonia was added to hydrolyze the residue. Product was extracted with four 5 ml volumes of diethyl ether, evaporated to dryness, and dissolved in 1.5 ml isopropanol-2M aqueous ammonia-methanol (7:1:2). tBoc-LysAMP- AMC (yield = 20.6%) was purified twice by silica gel column chromatography using a 10 x 1 cm column. Peak material was analyzed by MALDI-MS and NMR. MALDI was performed on an Applied Biosystems Voyager System 6235 in negative ion mode using 3- hydroxypicolinic acid (observed mass = 733.79; calculated mass = 734.26). 31P, 13C and 1H NMR data were collected using a 15 mm probe with the compound in DMSO. 1NMR (50OmHz, DMSO-J15, 5O0C) delta = 10.93 (s, IH), 10.85 (s, IH), 8.47 (s, IH), 8.12 (s, IH), 7.81 (d, J=2.0 Hz, IH), 7.71 (d, J=8.5 Hz, IH), 7.53 (d, J=8.8 Hz, IH), 7.35-7.44 (m, 2H), 7.27 (d, J=7.6 Hz, IH), 7.10-7.16 (m, IH), 6.25 (d, J=I.2 Hz, IH), 5.89 (d, J=5.4 Hz, IH), 5.57-5.62 (m, IH), 4.55-4.59 (m, IH), 4.18-4.21 (m, IH), 4.07-4.21 (m, IH), 4.02-4.05 (m, IH), 3.83-3.88 (m, IH), 3.74-3.80 (m, IH), 2.72-2.77 (m, IH), 2.66-2.70 (m, IH), 2.36 (d, J= 4.2 Hz, 3H), 1.64-1.70 (m, IH), 1.57-1.61 (m, IH), 1.33 (d, J=13.9 Hz, 9H), 1.23- 1.25 (m, IH), 1.00 (d, J= 6.1 Hz, 3H); 13C NMR (hmqc, DMSO-rf*, 5O0C, partial) delta = EPO <DP n="14"/>153.3, 126.5, 116.0, 112.7, 106.2, 87.5, 84.4, 74.5, 71.3, 64.3, 41.5, 40.3, 31.6, 28.8, 28.6, 28.1, 26.0, 18.6; 31P NMR (30OmHz, DMSO-J6) delta = 2.66. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
In ethanol; | ADP (Bu3NH+)2, AMP (Bu3NH+)2 and UMP (Bu3NH+)2 were prepared from the corresponding free acid and tributylamine (Bu3N; 2 eq) in EtOH |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With 3Na(1+)*P(18)O4(3-)=Na3P(18)O4;succinyl-CoA synthetase; at 20℃; for 0.05h;pH 8.1;Enzymatic reaction; Glycylglycine buffer; | Example 1: Synthesis of [gamma18O3]ATP Bacterial succinyl-CoA synthetase (an ammonium sulphate suspension) was diluted in 100 mM glycylglycine buffer, pH 8.1 containing 10 mM MgC12. Based on leading experiments for the synthesis of (gamma32P)ATP the reaction with Na3P18O4 was carried out with 1 or 2 enzyme Units per 50 mul total volume of the reaction solution which includes (final concentrations of) 100 mM glycylglycine buffer (pH 8.1), 10 mM MgCl2, 2.5 mM ADP, 100 muM succinyl-CoA. The reaction was started by the addition of 50 nmol Na3P18O4 and left at RT for 3 min. Reaction stop was by addition of 10 mul I N HC1 and samples were stored at 4C until purification by HPLC. The samples were purified by HPLC-system using a C2/C18-column (muRPC) preequilibrated with Triethylamine/acetic acid buffer (pH 7.0) (buffer A) containing 4 mM Triethylamine, 10 mM acetic acid, 0.25% methanol. The column effluent was monitored by spectrophotometrically due to the adsorption maxima of ATP and ADP purine rings at at 258 nm wavelength. Na3P18O4-samples diluted with bidest. water up to 2 ml were injected through a sample loop and the column continuously washed with buffer A until stable baseline was reached. Subsequently, elution of ATP and thereby separation from ADP in the sample was achieved by Triethylamine/acetic acid buffer (pH 5.5) (buffer B) containing 24 mM Triethylamine, 100 mM acetic acid, 30% methanol. A typical elution profile for the ATP separation is given in the Figure below. It shows start of the elution at 9% buffer B and upon application of the buffer gradient ATP gets eluted at 19% buffer B (6 ml elution volume). For determining crop of such [gamma18O3]ATP purification, parallel runs under identical conditions were performed with 16O-ATP/ADP standards. Upon 20 repeats of the HPLC-purification runs yields of 100-125 nmol [gamma18O3]ATP were obtained, respectively. The [gamma18O3]ATP fraction being in 80 mM Triethylamine-acetate buffer was further treated to remove the volatile buffer by vacuum centrifugation (Speedvac) until dryness. Then the sample was dissolved in 300mul bidest. water, deep frozen and finally lyophilized under high vacuum. The [gamma18O3]ATP preparations were kept at -80C until use, e.g. as the cosubstrate for protein phosphorylation. | |
With 3Na(1+)*P(18)O4(3-)=Na3P(18)O4; succinyl-CoA synthetase; magnesium chloride; at 20℃; for 0.05h;pH 8.1;Enzymatic reaction; glycylglycine buffer; | Bacterial succinyl-CoA synthetase (an ammonium sulphate suspension) was diluted in 100 mM glycyl glycine buffer, pH 8.1 containing 10 mM MgCl2. Based on leading experiments for the synthesis of (gamma32Rho)AlphaTauRho, the reaction with Na3P18O4 was carried out with 1 or 2 enzyme Units per 50 mu total volume of the reaction solution which includes (final concentrations of) 100 mM glycylglycine buffer (pH 8.1), 10 mM MgCl2, 2.5 mM ADP, 100 muMu succinyl-CoA. The reaction was started by the addition of 50 nmol Na3P18O4 and left at RT for 3 min. Reaction stop was by addition of 10 mu1 1 N HC1 and samples were stored at 4C until purification by HPLC.The samples were purified by HPLC-system using a C2/C18-column ^RPC) preequiiibrated with Triethylamine/acetic acid buffer (pH 7.0) (buffer A) containing 4 mM Triethylamine, 10 mM acetic acid, 0.25% methanol. The column effluent was monitored by spectrophotometrically due to the adsorption maxima of ATP and ADP purine rings at at 258 nm wavelength. Na3P18O4-samples diluted with bidest. water up to 2 ml were injected through a sample loop and the column continuously washed with buffer A until stable baseline was reached. Subsequently, elution of ATP and thereby separation from ADP in the sample was achieved by Triethylamine/acetic acid buffer (pH 5.5) (buffer B) containing 24 mM Triethylamine, 100 mM acetic acid, 30% methanol. A typical elution profile for the ATP separation is given in the Figure below. It shows start of the elution at 9% buffer B and upon application of the buffer gradient ATP gets eluted at 19% buffer B (6 ml elution volume). For determining crop of such [gamma18O3]AlphaTauRho purification, parallel runs under identical conditions were performed with 16O-ATP/ADP standards. Upon 20 repeats of the HPLC-purification runs yields of 100-125 nmol [gamma18O3]AlphaTauRho were obtained, respectively.The [gamma18O3]ATP fraction being in 80 mM Triethylamine-acetate buffer was farther treated to remove the volatile buffer by vacuum centrifugation (Speed vac) until dryness. Then the sample was dissolved in 300mu1 bidest. water, deep frozen and finally lyophilized under high vacuum. The [gamma18O3]AlphaTauRho preparations were kept at -80C until use, e.g. as the cosubstrate for protein phosphorylation. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With recombinant galactokinase from Streptococcus pneumoniae TIGR4; magnesium chloride; at 45℃; for 3h;pH 8;aq. buffer; Enzymatic reaction;Kinetics; | General procedure. The activity of recombinant GalKSpe4 toward Gal, Glc, N-acetylgalactosamine (GalNAc) and N-acetylglucosamine (GlcNAc) was assayed in a cocktail containing 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 5 mM <strong>[56-65-5]ATP</strong> and proper amount of GalKSpe4 at 45 C for 3 h. The reaction was terminated by boiling the mixture for 5 min followed by centrifugation. The supernatant was analyzed by normal phase silica gel thin-layer chromatography with the phase being n-butanol/acetic acid/water (2:1:1, v/v/v). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With recombinant galactokinase from Streptococcus pneumoniae TIGR4; magnesium chloride; at 45℃; for 3h;pH 8;aq. buffer; Enzymatic reaction;Kinetics; | The activity of protein GalKSpe4 toward Gal was assayed as described before11 with a little modification. Briefly, the reaction mixture containing Gal (8 mM), <strong>[56-65-5]ATP</strong> (10 mM), MgCl2 (5 mM), and GALK (6 muM) in Tris-HCl buffer (20 mM, pH 8.0) was incubated at 45 C for 180 min. The reducing sugar consumed in this reaction was quantified by the DNS method with d-Gal as standard.26 The effects of temperature (25-50 C) and pH (3.0-11.0) on the activity of GalKSpe4 were determined using Gal as the substrate. Kinetic data were obtained by determining the slope of linear phase of the progress curve over 2 min in 30 s intervals and then by calculating the kinetic parameters as described by Yang et 12 |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With recombinant galactokinase from Streptococcus pneumoniae TIGR4; magnesium chloride; at 45℃; for 3h;pH 8;aq. buffer; Enzymatic reaction; | General procedure. The activity of recombinant GalKSpe4 toward Gal, Glc, N-acetylgalactosamine (GalNAc) and N-acetylglucosamine (GlcNAc) was assayed in a cocktail containing 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 5 mM <strong>[56-65-5]ATP</strong> and proper amount of GalKSpe4 at 45 C for 3 h. The reaction was terminated by boiling the mixture for 5 min followed by centrifugation. The supernatant was analyzed by normal phase silica gel thin-layer chromatography with the phase being n-butanol/acetic acid/water (2:1:1, v/v/v). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With recombinant galactokinase from Streptococcus pneumoniae TIGR4; magnesium chloride; at 45℃; for 3h;pH 8;aq. buffer; Enzymatic reaction;Kinetics; | General procedure. The activity of recombinant GalKSpe4 toward Gal, Glc, N-acetylgalactosamine (GalNAc) and N-acetylglucosamine (GlcNAc) was assayed in a cocktail containing 50 mM Tris-HCl (pH 8.0), 5 mM MgCl2, 5 mM <strong>[56-65-5]ATP</strong> and proper amount of GalKSpe4 at 45 C for 3 h. The reaction was terminated by boiling the mixture for 5 min followed by centrifugation. The supernatant was analyzed by normal phase silica gel thin-layer chromatography with the phase being n-butanol/acetic acid/water (2:1:1, v/v/v). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
Carried out as follows: (i) 5 mM aqueous <strong>[56-65-5]ATP</strong> ((1) retention time 3.93 min) was stirred with excess sodium periodate to give ribose-oxidised dialdehyde-<strong>[56-65-5]ATP</strong> ((2) 4.06 min); (ii) The pH of the mixture was adjusted to 4.5 and a concentratedsolution of biotin-LC-hydrazide (3) in DMSOwas slowly added over 30 min, with vigorous stirring. HPLC analysis after a further hour showed the presence of biotin-LC-<strong>[56-65-5]ATP</strong> (4) at 3.69 min; (iii) the periodate was quenched with sodium borohydride (3.87 min) and the Tris-HCl added to 50 mM, pH 8.0; (iv) finally, Llysine (to 2 mM), MgCl2 (10 mM), ZnCl2 (160 lM), LysU (10 lM), inorganic pyrophosphatase (Sigma-Aldrich; 6 U/mL) was added in sequence and the mixture warmed to 37 C. Aqueous <strong>[56-65-5]ATP</strong> (to 6 mM) was then added in four portions over the period of 1 h and resulting mixture left for a further hour to give biotin-LC-Ap4A (6) as the majority product (4.24 min); (v) purification was easilycarried out by SOURCE-15Q/TEAB ion exchange HPLC as previously described24 and combined product fractions lyophilised to a highly hydroscopic, white crystalline solid, before storage at -20 C. Major side products from this reaction included Ap3A, ADP and 4. Compound 5 was identified by ESI-MS: [M-H]-1185.7 m/z, expected (C36H52N15O21P4S-) 1186.2 m/z and 31P NMR (202 MHz,D2O, 21500x) delta -11.63 (2P, m, Jalphabeta/deltagamma 22.2, Palpha,delta), -23.16 (1P, d, Jgammadelta 18.2, Pgamma), -23.28 (1P, d, Jbetaalpha 24.2, Pbeta), purity confirmed as >95% by HPLC. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: To a solution of nucleoside 5?-phosphoropiperidates (1-4, 0.1mmol) in N-methylpyrrolidone (2mL) were added NDPs (0.05mmol, the content of Bu3N was 2.0equiv) and DCI (0.25mmol). The reaction was stirred at 40C for 8h. Then, diethyl ether (20mL) was added into the solution, and the resulting white precipitate was collected by centrifuge. The crude products were dissolved in deionized H2O (1mL) and loaded onto an ion exchange gel column. Elution with NH4HCO3 buffer (linear gradient 0.2-0.5M), combination of appropriate fractions, and lyophilization gave Np3N?s as the ammonium salts. Passage of the solution of the ammonium salts in deionized H2O through a bed of Dowex 50W-X8 ion exchange resin (Na+ form) and lyophilization afforded dinucleoside triphosphate trisodium salts (16-18) as white solids. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
General procedure: To a solution of nucleoside 5?-phosphoropiperidates (1-4, 0.1mmol) in N-methylpyrrolidone (2mL) were added NDPs (0.05mmol, the content of Bu3N was 2.0equiv) and DCI (0.25mmol). The reaction was stirred at 40C for 8h. Then, diethyl ether (20mL) was added into the solution, and the resulting white precipitate was collected by centrifuge. The crude products were dissolved in deionized H2O (1mL) and loaded onto an ion exchange gel column. Elution with NH4HCO3 buffer (linear gradient 0.2-0.5M), combination of appropriate fractions, and lyophilization gave Np3N?s as the ammonium salts. Passage of the solution of the ammonium salts in deionized H2O through a bed of Dowex 50W-X8 ion exchange resin (Na+ form) and lyophilization afforded dinucleoside triphosphate trisodium salts (16-18) as white solids. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With dihydrogen peroxide; acetic acid; In water; at 20℃; for 312h; | 0029] To a 500 mL four-necked flask were added 8.54 g of adenosine 5?-diphosphate with a product code of 590-29413,commercialized by Wako Pure Chemical Industry, Ltd., Osaka, Japan, 28 mL of refined water, and 84 mL of acetic acid.While stirring at ambient temperature, the resulting mixture was then added with 28 mL of 30% hydrogen peroxidesolution over two minutes, and further stirred at ambient temperature for 13 days. Thereafter, the resulting mixture wasadmixed with 280 mL of acetone over 20 min under ice-chilling conditions, and further stirred for one hour. The resultingreaction product was collected by suction filtration and washed with 40 mL of acetone, followed by drying the resultingsolids in vacuo in a desiccator. Then, 5.8 g of the solids was dissolved in 20 mL of water and admixed with 116 mL ofacetone to effect crystallization. The obtained crystals were collected by suction filtration to obtain 4.76 g of 5?-adenosinediphosphate N1-oxide, which was then purified on column chromatography to obtain 5?-adenosine diphosphate N1-oxidewith a purity of 98% or higher.[0030] 5?-Adenosine triphosphate N1-xide with a purity of 98% or higher was obtained similarly as in the above procedureexcept for replacing the above adenosine 5?-diphosphate with adenosine 5?-triphosphate with a product code ofP0756L, commercialized by New England Biolabs Japan Inc., Tokyo, Japan. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With DL-dithiothreitol; full length cyclic GMP-AMP synthase; sodium chloride; magnesium chloride; dsDNA; In glycerol; at 37℃; for 0.666667h;Enzymatic reaction;Kinetics; Catalytic behavior; Mechanism; | Purified recombinant full length (fl, amino acids 1-507) and truncated (tr, amino acids 147-507) murine cGAS, including truncated mutant versions 1-6, were incubated in 20 mu, reactions containing: 1 muMu cGAS, 3.3 muMu dsDNA, 5 mM MgCl2, 150 mM NaCl, 20 mM Tris- HCl, pH 7.5 at 25C, 1 mM DTT, 10% glycerol, 1 mM each of nucleotides (typically ATP and GTP), and a32P or gamma32Rho radiolabeled NTPs or dNTPs at 37C for 40 min. Reactions were stopped by addition of 20 of 50 mM EDTA. 2 mu^of reaction solution was spotted onto high- performance TLC plates (HPTLC silica gel, 60 A pores, F254, 10x10 cm, cat 1.05628.0001, EMD Millipore) and products were separated with Solvent 1 (NH4HC03:C2H5OH:H20 [0.2 M:30%:70%], w:v:v) or 2 (NH4HC03:C2H5OH:H20 [0.025 M:30%:70%], w:v:v) at 25 C for 1 h. Reaction products were visualized by UV (254 nm) and phosphorimaging (Typhoon FLA 9500, GE Healthcare). Images were processed using Adobe Photoshop and Illustrator CS5. The TLC conditions used were largely based on a protocol established to separate 3 ',5' cAMP (Higashida et al, 2012). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
In aq. buffer; at 20℃; for 3h; | 1 mL of 1 mL of N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid (HEPES) buffer (100 mM, pH 7.4) containing 3 mM adenosine diphosphate (ADP) was added 1 mL of 3 mM Tb (NO3)3Aqueous solution, and then an aqueous solution of 2 mL of phenanthroline (Phen) at a concentration of 1.5 mM was added. The mixed solution was stirred at room temperature for 3 h and centrifuged at 10000 rpm for 20 min. The precipitate was washed with deionized water to remove unreacted reagent, centrifuged, The wash was repeated three times with deionized water. Finally, the precipitate was dried in an oven at 70 C, dried and stored in a desiccator |
Yield | Reaction Conditions | Operation in experiment |
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With water; zirconium(IV) oxide; at 80℃; for 48h; | (0117) A 10-mL vial was loaded with 0.33 g of NAD+, 0.29 g of zirconium dioxide (Zr02) . The powders were dissolved/dispersed with 9.5 mL of distilled water, and the mixture was heated at 80 C for 48 h. Zr02 was removed by centrifugation (10,000 rpm for 30 min) using 29x32x25-cm HSCEN-204 centrifuge. (0118) The 31P-NMR demonstrated a small peak at -11.15 ppm, attributed to NAD+, a peak at -0.03 ppm attributed to beta- nicotinamide mononucleotide, a peak at 0.09 ppm attributed to adenosine, and two peaks at 0.027 and 0.3 ppm, attributed to the two P atoms of adenosine diphosphate (ADP) . |
Yield | Reaction Conditions | Operation in experiment |
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With 5?-adenosylcobalamin; full-length enzyme NrdJd-wt from Stackebrandtia nassauensis; 2'-deoxyguanosine 5'-triphosphate; magnesium chloride; Cleland's reagent; In aq. buffer; at 20℃;Enzymatic reaction;Kinetics; | General procedure: Specific enzyme activities were determined by measurement of the conversion of NDP to dNDP, catalyzed by the enzyme in the presence of different dNTPs as allosteric effectors. All enzymatic assays were performed in triplicates. Under standard conditions the assay contains 50 mmol liter-1 Tris (pH 8.0), 20 mmol liter-1 MgCl2, 50 mmol liter-1 DTT, 1.0 mmol liter-1 dATP, 2.0 mmol liter-1 CDP, 5.0 mumol liter-1 AdoCl, and between 2 and 5 mumol liter-1 enzyme ( 0.2-0.5 mg ml-1). In effector titration experiments, a concentration range from 4 to 1000 mumol liter-1 was applied, including a measurement without effector. In the four substrate assays, 0.5 mmol liter-1 of each substrate (ADP, CDP, GDP, UDP) were applied with 0.5 mmol liter-1 of the tested effector. The assays, performed in 50-mul scale, were incubated 15 or 30 min at room temperature and stopped by addition of 50 mul methanol. After addition of 200 mul water, the samples were analyzed via HPLC. 20 mul of thesample were injected onto a C18 column and run with the followingbuffer: 50 mmol liter-1 potassium Pi (pH 7.5), 10% (v/v) methanol, 0.25% (v/v) tetrabutylammonium hydroxide. The buffer was prepared with KH2PO4 by setting the pH value with KOH. The analytes were eluted in a linear gradient of methanol from 10 to 30% (v/v). |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With (E)-N-(4-(1-benzoylpiperidin-4-yl)butyl)-3-(pyridin-3-yl)acrylamide; nicotinamide phosphoribosyltransferase; water; at 37℃;Enzymatic reaction;Kinetics; | A calibration curve for adenosine 5'-tetraphosphate (Ap4) (Jena Bioscience) was prepared in 200 mu^ of 0.5 M perchloric acid (PC A) and 100 mM ammonium formate at Ap4 concentrations of 0.04 muMu, 0.08 muMu, 0.16 muMu, 0.3 muMu, 0.625 muMu, 1.25 muMu, 2.5 muMu, 6.25 muMu, 12.5 muMu, 25 muMu, 62.5 muMu, 125 muMu, 250 muMu, and 500 muMu. Calibration curve and study samples were run on an Accela HPLC/Thermo Scientific triple quadrupole mass spectrometer by positive electrospray ionization. 5 muL samples were injected onto a 3 x 50 mm, 3 muiotaeta Hypercarb column and separated using a linear gradient from 98% A (10 mM ammonium bicarbonate, pH 9.5) and 2% B (acetonitrile (ACN)) to 5% A and 95% B at 6.4 minutes at 0.6 mL/min. Multiple reaction monitoring was used to monitor transitions for Ap4 (m/z 588 136) and 13C1015N5-<strong>[56-65-5]ATP</strong> (m/z 523 -> 146) as an internal standard. Linear calibration curves were obtained using Xcalibur software to quantitate Ap4 in biological samples. Inorganic phosphate (Pi) was assayed using the PiColorLock Gold phosphate detection reagent (Innova Biosciences). (0193) [00148] To test the effects of NAMPT inhibitors on AP4 formation, human NAMPT (200 nM) was incubated with <strong>[56-65-5]ATP</strong> (2 mM) and vehicle (1% DMSO) or one of the NAMPT inhibitors FK- 866, CHS-828, or GNI-50 (1 muMu each) for increasing times at 37 C in TMD buffer. Samples (50 mu) were removed at the indicated times and quenched with 50 mu of 1M perchloric acid (PCA) and submitted for LC MS/MS to detect ADP and Ap4. Another sample (80 muL) was removed, frozen and subsequently assayed for Pi using the Pi ColorLock Gold assay kit. [00149] As described above, ADP, Pi, and Ap4 concentrations were measured after incubating NAMPT with <strong>[56-65-5]ATP</strong> and a NAMPT inhibitorsFK-866, CHS-828, or GNI-50. Surprisingly, these NAMPT inhibitors not only differentially modulated Ap4 formation, but this effect did not have a direct correlation with NTPase modulatory activity as observed through NAMPT' s <strong>[56-65-5]ATP</strong>ase activity. Incubation of human NAMPT (200 nM) with <strong>[56-65-5]ATP</strong> (2 mM) produced a time-dependent increase of Ap4 formation (1.04 muMu Ap4 per hr) (see FIG. 4C). The presence of NAMPT inhibitor FK-866 (at 1 muMu) had essentially no impact on Ap4 production (0.88 muMu Ap4 per hr). However, the NAMPT inhibitors CHS-828 and GNI-50 were markedly different from each other and from FK-866 with respect to their impact on NAMPT-mediated Ap4 production (see FIG. 4C). CHS-828 (1 muMu) nearly abolished Ap4 generation (0.88 muMu per hr), while GNI-50 stimulated Ap4 production approximately 1 9-fold (1.93 muMu per hr). Table 2 shows the impact of the NAMPT inhibitors on ADP, P and Ap4 formation. Notably, although FK-866 had the largest impact on ADP production (a 5.39-fold increase in ADP production as compared to vehicle control), it resulted in less than half the Ap4 of GNI-50. Moreover, Ap4 decreased with FK-866 as compared to vehicle control but increased with GNI-50 as compared to vehicle control. Table 2: Impact of NAMPT inhibitors on ADP, P;, and Ap4 formation by NAMPT (0194) (0195) [00150] The values in Table 4represent the mean production rates of ADP, Pi, or Ap4, or calculated values using those production rates, in muMu/hr. Values in parentheses represent standard deviations. Pi + Ap4 is the sum of Pi and Ap4 production rates, which corresponds to the ADP value if the Pi liberated during Ap4 hydrolysis has only two possible fates: free Pi and Ap4. ADP/(Pi + Ap4) is the ratio between ADP formation and combined Pi and Ap4 formation. |
Yield | Reaction Conditions | Operation in experiment |
---|---|---|
With [D]-sodium hydroxide In aq. phosphate buffer; water-d2 at 37℃; |
Tags: 58-64-0 synthesis path| 58-64-0 SDS| 58-64-0 COA| 58-64-0 purity| 58-64-0 application| 58-64-0 NMR| 58-64-0 COA| 58-64-0 structure
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H319 | Causes serious eye irritation |
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H362 | May cause harm to breast-fed children |
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H371 | May cause damage to organs |
H372 | Causes damage to organs through prolonged or repeated exposure |
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Code | Phrase |
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H401 | Toxic to aquatic life |
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H411 | Toxic to aquatic life with long-lasting effects |
H412 | Harmful to aquatic life with long-lasting effects |
H413 | May cause long-lasting harmful effects to aquatic life |
H420 | Harms public health and the environment by destroying ozone in the upper atmosphere |
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