53-84-9
- Product Name：beta-Diphosphopyridine nucleotide
- Molecular Formula：C21H27N7O14P2
- Purity：99%
- Molecular Weight：
Product Details;
CasNo： 53-84-9
Molecular Formula： C21H27N7O14P2
Appearance： White powder
Export High Quality beta-Diphosphopyridine nucleotide food grade 53-84-9 In Medicine
- Molecular Formula:C21H27N7O14P2
- Molecular Weight:663.431
- Appearance/Colour:White powder
- Melting Point:140 - 142oC
- PSA：340.71000
- LogP:-1.29620
53-84-9 Usage
Description
β-Nicotinamide adenine dinucleotide (NAD+) plays a major role in metabolism as a cofactor and mobile electron acceptor. NAD+ is a required oxidizing cosubstrate for many enzymes. It is reduced to NADH (Cat# N-035) which carries electrons to the electron transport chain for subsequent oxidative phorphorylation and ATP production. NAD+ is capable of donating ADP-ribose moieties to a protein, producing nicotinamide in the process. Sirtuin enzymes use NAD+ as a substrate to deacetylate proteins and direct activity between the nucleus and mitochondria. NAD+ is regenerated by fermentation and by oxidative phosphorylation.
Chemical Properties
Beta-Nicotinamide adenine dinucleotide is a hygroscopic white powder. It should be stored desiccated. Store in cool place. Keep container tightly closed in a dry and well-ventilated place. Recommended storage temperature -20°C.
Uses
β-Nicotinamide Adenine Dinucleotide is a coeznyme consisting of an adenine base and a nicotinamide base connected by a pair of bridging phosphate group. β-Nicotinamide Adenine Dinucleotide acts as a c oenzyme in redox reactions, as a donor of ADP-ribose moieties in ADP-ribosylation reactions and also as a precursor of the second messenger molecule cyclic ADP-ribose. β-Nicotinamide Adenine Dinucleot ide also acts as a substrate for bacterial DNA ligases and a group of enzymes called sirtuins that use NAD+ to remove acetyl groups from proteins.
Application
β-Nicotinamide adenine dinucleotide (β-NAD) is a cofactor of alcohol dehydrogenase and acts as a neuromodulator and an inhibitory neurotransmitter in visceral smooth muscles. The NAD/NADH ratio has a role in the regulation of intracellular redox potential. It thereby influences metabolic reactions in vivo. It has been used for the preparation of deacetylated tubulin. It has also been used for UDP-glucose-6-hydrogenase (UGDH) enzyme activity assay of orital fibroblast cell lysates.β-Nicotinamide adenine dinucleotide (NAD+) and β-Nicotinamide adenine dinucleotide, reduced (NADH) comprise a coenzyme redox pair (NAD+:NADH) involved in a wide range of enzyme catalyzed oxidation reduction reactions. In addition to its redox function, NAD+/NADH is a donor of ADP-ribose units in ADP-ribosylaton (ADP-ribosyltransferases; poly(ADP-ribose) polymerases ) reactions and a precursor of cyclic ADP-ribose (ADP-ribosyl cyclases).
Definition
ChEBI: β-Nicotinamide adenine dinucleotide (NAD) is the oxidized form of β-Nicotinamide Adenine Dinucleotide. It exists as an anion under normal physio-logic conditions. It is functionally related to a deamido-NAD zwitterion. It is a conjugate base of a NAD(+). It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
General Description
β-Nicotinamide adenine dinucleotide (NAD) is a ubiquitously found electron carrier and a cofactor. NAD+ contains an adenylic acid and a nicotinamide-5′-ribonucleotide group linked together by a pyrophosphate moiety. In NAD+ complexes, the enzyme-cofactor interactions are highly conserved.
Biological Activity
NAD+, known more formally as nicotinamide adenine dinucleotide, is a signaling molecule as well as a cofactor or substrate for many enzymes. It acts as an oxidizing agent, accepting electrons from other molecules while being converted to its reduced form, NADH. NAD+ is also essential for the activity of several enzymes, including poly(ADP)-ribose polymerases and cADP-ribose synthases. For example, it is used by some sirtuins to mediate protein deacetylation, producing O-acetyl-ADP-ribose and nicotinamide as well as the deacetylated protein.
Biochem/physiol Actions
β-Nicotinamide adenine dinucleotide (β-NAD) is an electron carrier and a cofactor, significantly involved in enzyme-catalyzed oxido-reduction processes and many genetic processes. NAD cycles between the oxidized (NAD+) and reduced (NADH) forms to maintain a redox balance necessary for continued cell growth. NAD is also involved in microbial catabolism. β-NAD acts as a substrate for various enzymes in several cellular processes.
Purification Methods
NAD is purified by paper chromatography or better on a Dowex-1 ion-exchange resin. The column is prepared by washing with 3M HCl until free of material absorbing at 260nm, then with water, 2M sodium formate until free of chloride ions and, finally, with water. NAD, as a 0.2% solution in water, is adjusted with NaOH to pH 8, and adsorbed onto the column, washed with water, and eluted with 0.1M formic acid. Fractions with strong absorption at 360nm are combined, acidified to pH 2.0 with 2M HCl, and cold acetone (ca 5L/g of NAD) is added slowly and with constant agitation. It is left overnight in the cold, then the precipitate is collected in a centrifuge, washed with pure acetone and dried under vacuum over CaCl2 and paraffin wax shavings [Kornberg Methods Enzymol 3 876 1957]. It has been purified by anion-exchange chromatography [Dalziel & Dickinson Biochemical Preparations 11 84 1966.] The purity is checked by reduction to NADH (with EtOH and yeast alcohol dehydrogenase) which has 340mn 6220 M-1cm-1. [Todd et al. J Chem Soc 3727, 3733 1957.] [pKa, Lamborg et al. J Biol Chem 231 685 1958.] The free acid crystallises from aqueous Me2CO with 3H2O and has m 140-142o. It is stable in cold neutral aqueous solutions in a desiccator (CaCl2) at 25o, but decomposes at strong acid and alkaline pH. Its purity is checked by reduction with yeast alcohol dehydrogenase and EtOH to NADH and noting the OD at 340nm. Pure NADH (see below) has 340 6.2 x 104 M-1cm-1, i.e. 0.1mole of NADH in 3mL and in a 1cm path length cell has an OD at 340nm of 0.207. [Beilstein 26 IV 3644.]
InChI:InChI=1/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/p-1/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
53-84-9 Relevant articles
Oxygen Activation and Electron Transfer in Flavocytochrome P450 BM3
Ost, Tobias W. B.,Clark, Jonathan,Mowat, Christopher G.,Miles, Caroline S.,Walkinshaw, Malcolm D.,Reid, Graeme A.,Chapman, Stephen K.,Daff, Simon
, p. 15010 - 15020 (2003)
In flavocytochrome P450 BM3, there is a conserved phenylalanine residue at position 393 (Phe393), close to Cys400, the thiolate ligand to the heme. Substitution of Phe393 by Ala, His, Tyr, and Trp has allowed us to modulate the reduction potential of the heme, while retaining the structural integrity of the enzyme's active site. Substrate binding triggers electron transfer in P450 BM3 by inducing a shift from a low- to high-spin ferric heme and a 140 mV increase in the heme reduction potential. Kinetic analysis of the mutants indicated that the spin-state shift alone accelerates the rate of heme reduction (the rate determining step for overall catalysis) by 200-fold and that the concomitant shift in reduction potential is only responsible for a modest 2-fold rate enhancement. The second step in the P450 catalytic cycle involves binding of dioxygen to the ferrous heme. The stabilities of the oxy-ferrous complexes in the mutant enzymes were also analyzed using stopped-flow kinetics. These were found to be surprisingly stable, decaying to superoxide and ferric heme at rates of 0.01-0.5 s-1. The stability of the oxy-ferrous complexes was greater for mutants with higher reduction potentials, which had lower catalytic turnover rates but faster heme reduction rates. The catalytic rate-determining step of these enzymes can no longer be the initial heme reduction event but is likely to be either reduction of the stabilized oxy-ferrous complex, i.e., the second flavin to heme electron transfer or a subsequent protonation event. Modulating the reduction potential of P450 BM3 appears to tune the two steps in opposite directions; the potential of the wild-type enzyme appears to be optimized to maximize the overall rate of turnover. The dependence of the visible absorption spectrum of the oxy-ferrous complex on the heme reduction potential is also discussed.
The Role of Adsorption in the Initial One-Electron Electrochemical Reduction of Nicotinamide Adenine Dinucleotide (NAD+)
Bresnahan, William T.,Elving, Philip J.
, p. 2379 - 2386 (1981)
The title reduction was investigated at pH 9.1 in several base electrolytes of varying surface activity in order to elucidate the role of adsorption of NAD+, its free radical, and the resulting dimer at the aqueous solution/mercury electrode interface.In the presence of electrolytes of low activity, NAD+ is adsorbed at potentials positive to its 1-e reduction (ca. -0.9 V vs.SCE); the electrochemically generated dimer, (NAD)2, is adsorbed positive of -1.20 and -1.32 V in 0.06 and 0.4 M KCl solutions, respectively.NAD+ undergoes both diffusion- and adsorption-controlled reduction; the former predominates on slow time scale experiments and the latter on fast time scales.From low concentration surfactant (0.06 and 0.1 M tetraethylammonium (Tea+) chloride) solutions, NAD+ is only adsorbed positive of -0.65 V and an adsorption-controlled prewave appears, indicating that an adsorbed layer of NAD. and/or (NAD)2 is formed on reduction of dissolved NAD+.From a high concentration (0.4 M) Tea+ solution, NAD+ is adsorbed positive of -0.66 V, but the adsorption-controlled prewave is suppressed and the reduction is entirely diffusion controlled.Under diffusion control, the heterogeneous rate constant for the title reduction is ca. 0.1 cm s-1 and the rate constant for dimerization of NAD. is ca. 3E6 M-1 s-1.
The Peroxidase-NADH Biochemical Oscillator. 1. Examination of Oxygen Mass Transport, the Effect of Light, and the Role of Methylene Blue
Olson, Dean L.,Scheeline, Alexander
, p. 1204 - 1211 (1995)
The peroxidase-NADH oscillator examined here initially consists of four chemical components.The well-mixed aqueous solution includes native horseradish peroxidase, reduced β-nicotinamide adenine dinucleotide (NADH), methylene blue (MB+), and dissolved oxygen combined in a semi-batch reactor under a set of standard conditions.In this system, the macroscopic appearance of the process of oxygen dissolution from the gas phase is dependent on k-m, the mass transport constant of oxygen out of solution.Additional details of oxygen mass transport are derived.The amplitude of oxygen oscillations is decreased by continuous illumination by the deuterium source of a diode array spectrophotometer.This attenuation effect of light is dependent on wavelengths =+ allows several damped oscillations of small amplitude.Subsequent addition of MB+ to the oscillator results in oscillations of much larger amplitude.MB+ is seen to either directly or indirectly enhance the conversion of peroxidase compound III to the native enzyme and then inhibit oxygen consumption, allowing the initiation of relatively large, prolonged oscillations.MB+ is seen to function either as a system catalyst, or as a peroxidase inhibitor in the oxidation of NADH by oxygen.
Synthesis of Nicotinamide Adenine Dinucleotide (NAD) from Adenosine Monophosphate (AMP)
Walt, David R.,Rios-Mercadillo, Victor M.,Auge, Jacques,Whitesides, George M.
, p. 7805 - 7806 (1980)
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NADH oxidase activity of Bacillus subtilis nitroreductase NfrA1: Insight into its biological role
Cortial, Sylvie,Chaignon, Philippe,Iorga, Bogdan I.,Aymerich, Stephane,Truan, Gilles,Gueguen-Chaignon, Virginie,Meyer, Philippe,Morera, Solange,Ouazzani, Jamal
, p. 3916 - 3922 (2010)
NfrA1 nitroreductase from the Gram-positive bacterium Bacillus subtilis is a member of the NAD(P)H/FMN oxidoreductase family. Here, we investigated the reactivity, the structure and kinetics of NfrA1, which could provide insight into the unclear biological role of this enzyme. We could show that NfrA1 possesses an NADH oxidase activity that leads to high concentrations of oxygen peroxide and an NAD+ degrading activity leading to free nicotinamide. Finally, we showed that NfrA1 is able to rapidly scavenge H2O2 produced during the oxidative process or added exogenously. Structured summary: MINT- 7990140: nfrA1 (uniprotkb:. P39605) and nfrA1 (uniprotkb:. P39605) bind (MI:. 0407) by X-ray crystallography (MI:. 0114).
Rate-limiting one-electron transfer in the oxidation of NADH by polyoxometalates
Keita, Bineta,Essaadi, Khalid,Nadjo, Louis,Desmadril, Michel
, p. 411 - 418 (1995)
The kinetics of NADH oxidation by 3 Dawson-type mixed heteropolyanions were studied in buffered aqueous pH = 7 medium, by the stopped flow technique and UV-visible spectroscopy.The log of k was a linear function of the E0 of the first redox systems of the heteropolyanions with a slope of 16.5 V-1.The results indicate that, in the present case, the oxidation of NADH proceeds by a multistep mechanism involving initial rate-limiting one-electron transfer.An estimate of the E0 value for the one-electron NADH/NADHcation radical couple has been obtained.
The Peroxidase-NADH Biochemical Oscillator. 2. Examination of the Roles of Hydrogen Peroxide and Superoxide
Olson, Dean L.,Scheeline, Alexander
, p. 1212 - 1217 (1995)
The peroxidase-NADH oscillator examined here initially consists of a well-mixed aqueous solution of native horseradish peroxidase, reduced β-nicotinamide adenine dinucleotide (NADH), methylene blue (MB+), and dissolved oxygen combined in a semi-batch reactor under a set of standard conditions.Hydrogen peroxide and superoxide have been implicated as important chemical intermediates.A comprehensive model which includes such intermediates and all initial chemical species has appeared elsewhere.To experimentally explore the role of hydrogen peroxide in the oscillator, H2O2 was substituted for MB+ as an initial ingredient.This substitution allows relatively small, quasi-sinusoidal oscillations sensitive to the oxygen mass transport constant, and predicted earlier in a theoretical model.The oscillations become much larger when MB+ is added, suggesting that MB+ might serve as a chemical mediator between the small oscillations seen when H2O2 is substituted for MB+, and the relatively large oscillations observed when MB+ is present.Catalase and superoxide dismutase are used as enzymatic scavengers for H2O2 and O2.-, respectively.The enzymes are added individually to a working oscillator at oxygen minima and maxima to examine the roles and approximate the concentrations of H2O2 and O2.-.For the enzyme addition experiments, a perturbation model for oxygen behavior is proposed and applied to the interpretation of experimental data.Two methods of analysis for the addition of the enzyme probes indicate a higher concentration of H2O2 and O2.- at oxygen maxima than at minima.Comparison of experimental and simulated data indicate that the relatively simple model presented here is a resonable, yet apparently incomplete, representation of oxygen dynamics for the addition of scavenger enzymes to this oscillator.
Formation of pyridine nucleotides under symbiotic and non-symbiotic conditions between soybean nodules and free-living rhizobia
Tezuka, Takafumi,Murayama, Yuko
, p. 637 - 644 (2002)
Enzymatic regulation of pyricline nucleotide formation, under symbiotic and non-symbiotic conditions, was analyzed using soybeans (Glycine max L, cv. 'Akisengoku') and rhizobia (Bradyrhizobia japonicum strain A1017), respectively. It was found that levels
Magneto-stimulated hydrodynamic control of electrocatalytic and bioelectrocatalytic processes.
Katz, Eugenii,Willner, Itamar
, p. 10290 - 10291 (2002)
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Poly(aniline)-poly(acrylate) composite films as modified electrodes for the oxidation of NADH
Bartlett, Philip N.,Simon, Evelyne
, p. 2599 - 2606 (2000)
Poly(aniline), electrochemically deposited on an electrode surface in the presence of poly(acrylic acid), forms a film which remains protonated, and conducting, at pH 7. The resulting modified electrode is an electrocatalytic surface for NADH oxidation at +0.05 V vs. SCE in 0.1 M citrate-phosphate buffer at pH 7. The amperometric responses of these composite poly(aniline) films for NADH oxidation were studied in detail and fitted to a kinetic model in which the NADH diffuses into the polymer film and then binds to catalytic sites within the film where it undergoes reduction to NAD+. The rate determining process depends on the concentration of NADH present and the polymer film thickness. A comparison of the results presented here for the poly(aniline)-poly(acrylate) films with earlier work on poly(aniline)-poly(vinylsulfonate) films shows that the currents obtained for NADH at these poly(aniline)-poly(acrylate) films are approximately one third of those obtained for the poly(aniline)-poly(vinylsulfonate) films under similar conditions, that the currents saturate at lower NADH concentration and that the response is less stable towards repeated measurements. The poly(aniline)-poly(acrylate) films are, however, less readily inhibited by NAD+ and possess the potential advantage that the carboxylate groups can be used as sites for chemical attachment of enzymes or NADH derivatives by using simple coupling reactions.
Altering the substrate specificity of glutamate dehydrogenase from Bacillus subtilis by site-directed mutagenesis
Khan, Md. Iqbal Hassan,Kim, Hyeung,Ashida, Hiroyuki,Ishikawa, Takahiro,Shibata, Hitoshi,Sawa, Yoshihiro
, p. 1802 - 1805 (2005)
The Lys80, Gly82 and Met101 residues of glutamate dehydrogenase from Bacillus subtilis were mutated into a series of single mutants. The wild-type enzyme was highly specific for 2-oxoglutarate, whereas G82K and M101S dramatically switched to increased specificity for oxaloacetate with k cat values 3.45 and 5.68s-1, which were 265-fold and 473-fold higher respectively than those for 2-oxoglutarate.
Switching the Mechanism of NADH Photooxidation by Supramolecular Interactions
Mengele, Alexander K.,Weixler, Dominik,Chettri, Avinash,Maurer, Maite,Huber, Fabian Lukas,Seibold, Gerd M.,Dietzek, Benjamin,Eikmanns, Bernhard J.,Rau, Sven
supporting information, p. 16840 - 16845 (2021/10/25)
A series of three Ru(II) polypyridine complexes was investigated for the selective photocatalytic oxidation of NAD(P)H to NAD(P)+ in water. A combination of (time-resolved) spectroscopic studies and photocatalysis experiments revealed that ligand design can be used to control the mechanism of the photooxidation: For prototypical Ru(II) complexes a 1O2 pathway was found. Rudppz ([(tbbpy)2Ru(dppz)]Cl2, tbbpy=4,4'-di-tert-butyl-2,2'-bipyridine, dppz=dipyrido[3,2-a:2′,3′-c]phenazine), instead, initiated the cofactor oxidation by electron transfer from NAD(P)H enabled by supramolecular binding between substrate and catalyst. Expulsion of the photoproduct NAD(P)+ from the supramolecular binding site in Rudppz allowed very efficient turnover. Therefore, Rudppz permits repetitive selective assembly and oxidative conversion of reduced naturally occurring nicotinamides by recognizing the redox state of the cofactor under formation of H2O2 as additional product. This photocatalytic process can fuel discontinuous photobiocatalysis.
Fluorescent half-sandwich phosphine-sulfonate iridium(III) and ruthenium(II) complexes as potential lysosome-targeted anticancer agents
Du, Qing,Yang, Yuliang,Guo, Lihua,Tian, Meng,Ge, Xingxing,Tian, Zhenzhen,Zhao, Liping,Xu, Zhishan,Li, Juanjuan,Liu, Zhe
, p. 821 - 830 (2018/11/23)
The synthesis, characterization and biological activity of neutral fluorescent Ir(III) and Ru(II) half-sandwich organometallic complexes containing phosphine-sulfonate ligands are reported. X-ray crystal structure of complexes 1–3, 10 and 11 exhibits the expected half-sandwich “three-legged piano-stool” pseudo-octahedral geometry. Spectroscopic properties study displays that these complexes show rich fluorescence properties. With the exception of 9, 10 and 11 toward A549 human lung cancer cells and 10 towards HeLa human cervical cancer cells, each complex shows promising cytotoxicity toward HeLa and A549 cells line with IC50 values in the range of 3.6–53.1 μM, and 6.5–34.5 μM, respectively. Hydrolysis, DNA cleavage and depolarization of the mitochondrial membrane potential (MMP) appear not to be the main mechanism of action. However, these complexes are able to covert NADH to NAD+ via the transfer hydrogenation. Mechanism studies by flow cytometry display that the complexes exert their anticancer efficacy by inducing apoptosis, perturbing the cell cycle and increasing the intracellular ROS level. Furthermore, fluorescence property of these complexes provides a tool to investigate the microscopic mechanism by confocal microscopy. Notably, the typical Ir(III) complex 3 can specially localize to lysosome and damage it. In addition, complex 3 enters into HeLa cells mainly through energy-dependent pathway.
Organometallic ruthenium and iridium phosphorus complexes: Synthesis, cellular imaging, organelle targeting and anticancer applications
Li, JuanJuan,Tian, Zhenzhen,Zhang, Shumiao,Xu, Zhishan,Mao, Xudong,Zhou, Yumin,Liu, Zhe
, (2019/02/20)
The use of metal complexes containing phosphorus ligands as anticancer agents has not been well studied. In this work, eight novel half-sandwich IrIII and RuII compounds with P^P-chelating ligands have been synthesized and fully characterized, and alongside two crystal structures were reported. All eight complexes displayed highly potent antiproliferative activity, up to nine times more potent than the clinical anticancer drug cisplatin towards A549 lung cancer cells. Complex Ir1, which has a simpler structure and highly potent antiproliferative activity, was selected to investigate in further mechanistic studies. No hydrolysis and nucleobase binding occurred for complex Ir1. In order to elucidate subcellular localization, the self-luminescence of the complex Ir1 was utilized. Ir1 can specifically target lysosomes and facilitate excessive production of reactive oxygen species, resulting in lysosomal membrane permeabilization in A549 cells. Release of cathepsin B and changes in the mitochondria membrane potential also contributed to the observed cytotoxicity of Ir1, which demonstrated an anticancer action mechanism that was different from that of cisplatin. The favorable results from biological and chemical research demonstrated that these types of complexes hold significant theranostic potential.
Toward Automated Enzymatic Glycan Synthesis in a Compartmented Flow Microreactor System
Heinzler, Raphael,Fisch?der, Thomas,Elling, Lothar,Franzreb, Matthias
supporting information, p. 4506 - 4516 (2019/08/20)
Immobilized microfluidic enzyme reactors (IMER) are of particular interest for automation of enzyme cascade reactions. Within an IMER, substrates are converted by paralleled immobilized enzyme modules and intermediate products are transported for further conversion by subsequent enzyme modules. By optimizing substrate conversion in the spatially separated enzyme modules purification of intermediate products is not necessary, thus shortening process time and increasing space-time yields. The IMER enables the development of efficient enzyme cascades by combining compatible enzymatic reactions in different arrangements under optimal conditions and the possibility of a cost-benefit analysis prior to scale-up. These features are of special interest for automation of enzymatic glycan synthesis. We here demonstrate a compartmented flow microreactor system using six magnetic enzyme beads (MEBs) for the synthesis of the non-sulfated human natural killer cell-1 (HNK-1) glycan epitope. MEBs are assembled to build compartmented enzyme modules, consisting of enzyme cascades for the synthesis of uridine 5′- diphospho-α- d-galactose (UDP-Gal) and uridine 5′-diphospho-α-d-glucuronic acid (UDP-GlcA), the donor substrates for the Leloir glycosyltransferases β4-galactosyltransferase and β3-glucuronosyltransferase, respectively. Glycan synthesis was realized in an automated microreactor system by a cascade of individual enzyme module compartments each performing under optimal conditions. The products were analyzed inline by an MS-system connected to the microreactor. The high synthesis yield of 96% for the non-sulfated HNK-1 glycan epitope indicates the excellent performance of the automated enzyme module cascade. Furthermore, combinations of other MEBs for nucleotide sugars synthesis with MEBs of glycosyltransferases have the potential for a fully automated and programmed glycan synthesis in a compartmented flow microreactor system. (Figure presented.).
53-84-9 Process route
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- 58-68-4,443892-10-2
NADH
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- 53-84-9,66844-06-2
NAD
| Conditions | Yield |
|---|---|
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With oxygen; coenzyme PQQ; In water; at 30 ℃; Rate constant; pH 6.7; other catalysts, without and with diaphorase;
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With oxygen; In water; at 25 ℃; Mechanism; Irradiation; biochemical oscillator with horseradish peroxidase; effect of light, role of methylene blue added; pH 5.10 (sodium acetate buffer);
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With oxygen; In water; at 25 ℃; Mechanism; biochemical oscillator with horseradish peroxidase; effects of catalase and superoxide dismutase enzymes added, roles of hydrogen peroxide and methylene blue added; pH 5.10 (sodium acetate buffer);
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With α1P2W17VO628-; buffer pH=7; In water; at 20 ℃; under 760 Torr; Mechanism; Rate constant;
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With oxygen; diaphorase; pyrroloquinoline quinone; In water; at 30 ℃; pH 6.7;
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With mercury dichloride; In water; at 20 ℃; pH=7.4; Further Variations:; Reagents; Kinetics;
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With 4-oxo-TPO; Nitrite; Nitrogen dioxide; In phosphate buffer; pH=6.8; Kinetics; ambient temperature;
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With poly(aniline)-poly(vinyl sulfonate) modified electrode; In various solvent(s); at 25 ℃; pH=7.0; Kinetics; Electrochemical reaction;
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With flavocytochrome P450 BM3 wild type; In various solvent(s); at 15 ℃; pH=7.0; Further Variations:; Reagents; Enzyme kinetics;
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Fe3O4-[3-(2-aminoethyl)aminopropyl]trimethoxysilane-PQQ; In various solvent(s); pH=7.0; Kinetics; Electrochemical reaction;
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With poly(aniline)-poly(acrylate) film; In various solvent(s); at 25 ℃; Further Variations:; potentials; film thicknesses; Kinetics; Electrochemical reaction;
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With sfnoxK2 NADH oxidase from Lactobacillus sanfranciscensis; oxygen; In various solvent(s); at 30 ℃; pH=7; Further Variations:; Reagents; Kinetics; Enzyme kinetics; Enzymatic reaction;
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With Bacillus subtilis nitroreductase NfrA1; oxygen; ammonium bicarbonate; In water; at 37 ℃; pH=8.4; Enzymatic reaction;
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With human recombinant 3β-hydroxysteroid dehydrogenase/Delta 5->4 isomerase type 2; 5-androstenedione; at 27 ℃; pH=7.4; Concentration; Reagent/catalyst; Kinetics; aq. phosphate buffer;
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With Thermus thermophilus lactate dehydrogenase A75G mutant; sodium pyruvate; magnesium chloride; at 25 ℃; pH=7.5; Concentration; Reagent/catalyst; Temperature; Kinetics; aq. buffer; Enzymatic reaction;
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With sodium hydroxide; C20H24IrN2O3(1+)*0.5O4S(2-); In water; acetonitrile; at 25 ℃; Conversion of starting material;
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NADH; With 1-(4-hydroxy-3,5-dimethoxy-phenyl)-ethanone; triethylamine; In aq. acetate buffer; at 30 ℃; for 0.0833333h; pH=7;
With laccase from Myceliophthora thermophila; In aq. acetate buffer; Reagent/catalyst; pH-value; Catalytic behavior; Kinetics; Enzymatic reaction;
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With laccase from Myceliophthora thermophilia; oxygen; methylene blue; In aq. buffer; at 30 ℃; pH=7; Reagent/catalyst; Time; Catalytic behavior; Irradiation; Enzymatic reaction;
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With [(η5-pentamethylcyclopentadienyl)Ir(2-(4-hydroxyphenyl)pyridine)Cl]; In methanol; aq. phosphate buffer; at 36.84 ℃; for 24h; pH=7.5; Reagent/catalyst; Concentration; Catalytic behavior;
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With reduced flavin mononucleotide; In aq. phosphate buffer; at 30 ℃; pH=7; Reagent/catalyst; Wavelength; Catalytic behavior; Schlenk technique; Irradiation;
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With [(η5-C5Me4C6H4C6H5)Ir(2,6-diisopropyl-N-(quinolin-2-ylmethylene)aniline)Cl]PF6; In methanol; water; at 24.84 ℃; for 7.5h; Solvent; Reagent/catalyst; Temperature; Time;
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With alcohol dehydrogenase from Saccharomyces cerevisiae; acetaldehyde; Enzymatic reaction;
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With C32H42ClO3PRuS; In methanol; water; at 24.84 ℃; for 8h; Reagent/catalyst; Temperature; Solvent;
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With C37H41ClIrN4(1+)*Cl(1-); In methanol; water; at 24.84 ℃; for 7h; Kinetics;
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With [(η5‐1,2,3,4,5‐pentamethyl‐cyclopentadiene)Ir(1,2‐bis(diphenylphosphino)ethane)Cl]hexafluorophosphate; In methanol; water; at 24.84 ℃; for 8h; Catalytic behavior; UV-irradiation;
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With 1,4-dithio-D,L-threitol; NADH oxidase immobilized onto PureCube Ni-IDA MagBeads; In aq. buffer; pH=6.5; Catalytic behavior; Kinetics; Enzymatic reaction;
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With C33H33ClFeIrN; In methanol; water; at 24.84 ℃; for 8h; Reagent/catalyst; Catalytic behavior;
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With Mycobacterium smegmatis carveol dehydrogenase; 5-[(p-hydroxyphenyl)methyl]-4,4-dimethyl-2,3-pyrrolidinedione; Enzymatic reaction;
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With oxygen; [(4,4'-di-tert-butyl-2,2'-bipyridine)2Ru(dipyrido[3,2-a:2’,3’-c]phenazine)]Cl2; In water; for 2h; Reagent/catalyst; Catalytic behavior; Irradiation; Sealed tube;
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- 1094-61-7
nicotinamide mononucleotide
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- 24558-92-7
N,N'-dicyclohexyl-4-morpholinecarboxamidinium salt of adenosine-5'-phosphoromorpholidate
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- 53-84-9,66844-06-2
NAD
| Conditions | Yield |
|---|---|
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With magnesium sulfate; manganese(ll) chloride; In formamide; for 16h; Ambient temperature;
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58% |
53-84-9 Upstream products
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64363-04-8
ATP
-
53-84-9
NAD
-
865-05-4
3-(aminocarbonyl)-1-[5-O-[[1-(6-amino-9H-purin-9-yl)-1-deoxy-β-D-ribofuranos-5-O-yl]phosphonyloxy(oxylato)phosphinyl]-β-L-ribofuranosyl]pyridinium
-
10012-96-1
C21H28(2)HN7O14P2
53-84-9 Downstream products
-
75-07-0
acetaldehyde
-
47774-99-2
ADP‐ribofuranose
-
98-92-0
nicotinamide
-
68521-69-7
α-1-O-methyl-ADP-ribose
Relevant Products
-
Cyanocobalamin USP43CAS：68-19-9
-
-
Benzeneacetonitrile, alpha-phenyl-CAS：86-29-3
