1255150-40-3Relevant academic research and scientific papers
Clickable NAD analogues for labeling substrate proteins of poly(ADP-ribose) polymerases
Jiang, Hong,Kim, Jun Hyun,Frizzell, Kristine M.,Kraus, W. Lee,Lin, Hening
, p. 9363 - 9372 (2010)
Poly(ADP-ribose) polymerases (PARPs) catalyze the transfer of multiple adenine diphosphate ribose (ADP-ribose) units from nicotinamide adenine dinucleotide (NAD) to substrate proteins. There are 17 PARPs in humans. Several PARPs, such as PARP-1 and Tankyrase-1, are known to play important roles in DNA repair, transcription, mitosis, and telomere length maintenance. To better understand the functions of PARPs at a molecular level, it is necessary to know what substrate proteins PARPs modify. Here we report clickable NAD analogues that can be used to label PARP substrate proteins. The clickable NAD analogues have a terminal alkyne group which allows the conjugation of fluorescent or affinity tags to the substrate proteins. Using this method, PARP-1 and tankyrase-1 substrate proteins were labeled by a fluorescent tag and visualized on SDS-PAGE gel. Using a biotin affinity tag, we were able to isolate and identify a total of 79 proteins as potential PARP-1 substrates. These include known PARP-1 substrate proteins, including histones and heterogeneous nuclear ribonucleoproteins. About 40% of the proteins were also identified in recent proteomic studies as potential PARP-1 substrates. Among the identified potential substrates, we further demonstrated that tubulin and three mitochondrial proteins, TRAP1 (TNF receptorassociated protein 1), citrate synthase, and GDH (glutamate dehydrogenase 1), are substrates of PARP-1 in vitro. These results demonstrate that the clickable NAD analogue is useful for labeling, in-gel detection, isolation, and identification of the substrate proteins of PARPs and will help to understand the biological functions of PARPs.
Sequential one-pot synthesis of benzoxazoles from aryl bromides: Successive palladium- and copper-catalyzed reactions
Wu, Xiao-Feng,Neumann, Helfried,Neumann, Stephan,Beller, Matthias
, p. 3040 - 3042 (2013)
A convenient one-pot process has been developed for the synthesis of benzoxazoles. Starting from aryl bromides and 1,2-dibromobenzenes palladium-catalyzed aminocarbonylation and subsequent copper-catalyzed coupling reaction gave a variety of substituted benzoxazoles in moderate to good yields.
Synthesis of primary Amides via Copper-Catalyzed Aerobic Decarboxylative ammoxidation of Phenylacetic Acids and α-Hydroxyphenylacetic acids with Ammonia in water
Song, Qiuling,Feng, Qiang,Yang, Kai
, p. 624 - 627 (2014)
A Cu2O-catalyzed aerobic oxidative decarboxylative ammoxidation to primary benzamides from phenylacetic acids and a-hydroxyphenylacetic acids is developed. A variety of primary benzamides could be prepared smoothly, in good to excellent yields, by means of a one-pot domino protocol combining decarboxylation, dioxygen activation, oxidative C-H bond functionalization, and amidation reactions.
Selective hydration of nitriles to amides catalysed by PCP pincer supported nickel(ii) complexes
Borau-Garcia,Gutsulyak,Burford,Piers
, p. 12082 - 12085 (2015)
The (PCP)Ni-OH complexes 2R (R = iPr, tBu, Cy) are effective catalyst precursors for the selective hydration of nitriles to the corresponding amides under relatively mild conditions (80 °C) and low catalyst loadings (0.05-0.5%). Substrate scope includes aliphatic, vinylic and aromatic nitriles, but substrates with protic groups poison the catalyst abruptly. The catalysts are effective because the electron rich nature of the PCP ligands and their steric bulk renders the hydroxo group labile.
Incorporation of 13C glucose into nicotinamide in E. coli and in S. cerevisiae
Gupta,Hemscheidt,Sayer,Spenser
, p. 418 - 425 (2001)
The mode of incorporation into nicotinamide of label from 13C-labeled samples of D-glucose, in Escherichia coli and Saccharomyces cerevisiae, was determined by means of 13C NMR spectroscopy. The results, which confirm and extend early studies with radioactive tracers, permit a definitive choice to be made between alternative biogenetic proposals.
Nicotinamide riboside-amino acid conjugates that are stable to purine nucleoside phosphorylase
Hayat, Faisal,Migaud, Marie E.
, p. 2877 - 2885 (2020)
The nutraceutical Nicotinamide Riboside (NR), an efficacious biosynthetic precursor to NAD, is readily metabolized by the purine nucleoside phosphorylase (PNP). Access to the PNP-stable versions of NR is difficult because the glycosidic bond of NR is easily cleaved. Unlike NR, NRH, the reduced form of NR, offers sufficient chemical stability to allow the successful functionalisation of the ribosyl-moiety. Here, we report on a series of NRH and NR derived amino acid conjugates, generated in good to excellent yields and show that O5′-esterification prevents the PNP-catalyzed phosphorolysis of these NR prodrugs.
Transition state structure of the solvolytic hydrolysis of NAD+
Berti, Paul J.,Schramm, Vern L.
, p. 12069 - 12078 (1997)
The transition state structure has been determined for the pH- independent solvolytic hydrolysis of NAD+. The structure is based on kinetic isotope effects (KIEs) measured for NAD+'s labeled in various positions of the ribose ring and in the leaving group nitrogen. The KIEs for reactions performed at 100°C in 50 mM NaOAc (pH 4.0) were as follows: 1-15N, 1.020 ± 0.007; 1'-14C, 1.016 ± 0.002; [1-15N,1'-14C], 1.034 ± 0.002; 1'- 3H, 1.194 ± 0.005; 2'-3H, 1.114 ± 0.004; 4'-3H, 0.0997 ± 0.001; 5'3H, 1.000 ± 0.003; 4'-18O, 0.988 ± 0.007. The transition state structure was determined using bond energy/bond order vibrational analysis to predict KIEs for trial transition state models. The structure that most closely matches the experimental KIEs defines the transition state. A structure interpolation method was developed to generate trial transition state structures and thereby systematically search reaction coordinate space. Structures are generated by interpolation between reference structures, reactant NAD+ and a hypothetical {ribo-oxocarbenium ion plus nicotinamide} structure. The point in reaction coordinate space where all the predicted KIEs matched the measured ones was considered to locate the transition state structure. This occurred when the residual bond order to the leaving group nicotinamide, n(LG,TS), was 0.02 (bond length = 2.65 A?) and the bond order to the approaching nucleophile, n(Nu,TS), was 0.005 (3.00 A?). Thus, bond-breaking and bond-making in this A(N)D(N) reaction are asynchronous, and the transition state has a highly oxocarbenium ion-like character.
Supported silver nanoparticle catalyst for selective hydration of nitriles to amides in water
Mitsudome, Takato,Mikami, Yusuke,Mori, Haruhiko,Arita, Shusuke,Mizugaki, Tomoo,Jitsukawa, Koichiro,Kaneda, Kiyotomi
, p. 3258 - 3260 (2009)
Hydroxyapatite-supported silver nanoparticles (AgHAP) acted as a highly efficient reusable heterogeneous catalyst for hydration of diverse nitriles, including heteroaromatic ones, into amides in water.
Monomeric nickel hydroxide stabilized by a sterically demanding phosphorus-nitrogen PN3P-pincer ligand: synthesis, reactivity and catalysis
Yao, Changguang,Chakraborty, Priyanka,Aresu, Emanuele,Li, Huaifeng,Guan, Chao,Zhou, Chunhui,Liang, Lan-Chang,Huang, Kuo-Wei
, p. 16057 - 16065 (2018)
A terminal nickel hydroxide complex (PN3P)Ni(OH) (3) bearing the 2nd generation phosphorus-nitrogen PN3P-pincer ligand has been synthesized and structurally characterized. As a nucleophile, 3 reacts with CO to afford the hydroxycarbonyl complex 4, (PN3P)Ni(COOH). 3 can also activate CO2 and CS2 to produce nickel bicarbonate (PN3P)Ni(OCOOH) (5) and bimetallic dithiocarbonate [(PN3P)NiS]2CO (6) respectively, as well as to promote aryl isocyanate and isothiocyanate insertion into the Ni-OH bond to give the corresponding (PN3P)NiEC(O)NHAr complexes (E = O, 7; E = S, 8). In addition, 3 catalyzes the nitrile hydration to various amides with well-defined intermediates (PN3P)Ni-NHC(O)R (R = Me, 9; R = Ph, 10).
NOVEL ENZYMATIC CYCLIZATIONS OF PYRIDINE NUCLEOTIDE ANALOGS: CYCLIC-GDP-RIBOSE AND CYCLIC-HDP-RIBOSE
Zhang, Fang-Jie,Sih, Charles J.
, p. 9289 - 9292 (1995)
The cyclase of Aplysia californica catalyzed an alternative mode of cyclization of nicotinamide guanine dinucleotide (NGD) and nicotinamide hypoxanthine dinucleotide (NHD) to form cyclic-GDP-ribose (cGDPR) and cyclic-HDP-ribose (cHDPR) respectively.In these cyclic nucleotides, the newly formed glycosyl bonds are attached onto the N-7 nitrogen of the purine rings instead of the N-1 nitrogen as in cyclic ADP-ribose (cADPR).
