NADP+ (hydrate)
(Synonyms: Coenzyme II, β-NADP, Nicotinamide adenine dinucleotide phosphate, TPN) 目录号 : GC47740
A neuropeptide with diverse biological activities
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >90.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
NADP+ is the oxidized form of the electron donor nicotinamide adenine dinucleotide phosphate . It serves as a cofactor in various biological reactions.1,2 In addition, the balance between these reduced and oxidized forms plays key roles in diverse cellular functions, including cell survival, the maintenance of redox status, and intracellular signaling.2,3 For example, binding of NADP+ to β-subunits of Kv channels activates ion transport, whereas NADPH stabilizes channel inactivation.4 NADP+ is biosynthesized from NAD+ by NAD kinase, with ATP as the phosphoryl donor.5
1.Jackson, J.B.A review of the binding-change mechanism for proton-translocating transhydrogenaseBiochimica et Biophysica Acta1817(10)1839-1846(2012) 2.Nakamura, M., Bhatnagar, A., and Sadoshima, J.Overview of pyridine nucleotides review seriesCirc. Res.111(5)604-610(2012) 3.Ziegler, M.A vital link between energy and signal transduction: Regulatory functions of NAD(P)FEBS Journal272(18)4561-4564(2014) 4.Kilfoil, P.J., Tipparaju, S.M., Barski, O.A., et al.Regulation of ion channels by pyridine nucleotidesCirc. Res.112(4)721-741(2013) 5.Shi, F., Li, Y., Li, Y., et al.Molecular properties, functions, and potential applications of NAD kinasesActa Biochim. Biophys. Sin. (Shanghai)41(5)352-361(2009)
| Cas No. | N/A | SDF | |
| 别名 | Coenzyme II, β-NADP, Nicotinamide adenine dinucleotide phosphate, TPN | ||
| Canonical SMILES | O[C@H]1[C@@H](OP(O)(O)=O)[C@H](N2C=NC3=C2N=CN=C3N)O[C@@H]1COP(OP(OC[C@@H]4[C@@H](O)[C@@H](O)[C@H]([N+]5=CC(C(N)=O)=CC=C5)O4)([O-])=O)(O)=O | ||
| 分子式 | C21H28N7O17P3.XH2O | 分子量 | 743.4 |
| 溶解度 | PBS (pH 7.2): 10 mg/ml | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 1.3452 mL | 6.7259 mL | 13.4517 mL |
| 5 mM | 0.269 mL | 1.3452 mL | 2.6903 mL |
| 10 mM | 0.1345 mL | 0.6726 mL | 1.3452 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。
Interaction of NADPH-adrenodoxin reductase with NADP++ as studied by pulse radiolysis
Biochemistry 1995 Oct 10;34(40):12932-6.PMID:7548051DOI:10.1021/bi00040a003.
The reduction of flavin in NADH--adrenodoxin reductase by the hydrated electron (eaq-) was investigated by pulse radiolysis. The eaq- reduced directly the flavin of the reductase to form a blue semiquinone of the enzyme. Subsequently, the semiquinone decayed by dismutation to form the oxidized and fully reduced forms of the enzyme with a second-order rate constant of 4.4 x 10(4) M-1 s-1. In the presence of equimolar NADP++, the decay of eaq- accompanied an absorption increase at 400 nm, the spectrum of which, formed transiently, is identical to that of NADP+ radical (NADP+.). Subsequently, the transient species decayed concomitantly with the formation of the semiquinone. The rate constant in the formation of the semiquinone was independent of the concentration of the enzyme (6.1 x 10(4) s-1 at pH 7.5). From these results, it is concluded that eaq- reacts with NADP++ bound to the enzyme to form NADP+. initially, and subsequently, an electron flows from the NADP+. to the flavin by an intracomplex electron transfer. A similar result was obtained in the reaction of CO2- or N-methylnicotinamide radical with the NADP+(+)-adrenodoxin reductase complex. These results suggest that the nicotinamide moiety of NADP++ bound to the enzyme is accessible to the solvent and masks the flavin completely.
Functional and ligand binding studies of NAD(P)H hydrate dehydratase enzyme from vancomycin-resistant Staphylococcus aureus by NMR spectroscopic approach, including saturation transfer difference (STD-NMR) spectroscopy
Biochimie 2022 Oct;201:148-156.PMID:35716900DOI:10.1016/j.biochi.2022.06.004.
NADH and NADPH are labile coenzymes that undergo hydration by enzymatic reaction or by heat at 5,6 double bond, and convert into non-functional hydrates, NADHX and NADPHX, respectively. The NAD(P)H hydrate dehydratase enzyme catalyzes the dehydration of S-NADHX/S-NADPHX at the expense of ATP, and thus contributes in the nicotinamide nucleotide repair process. This enzyme is also known as "metabolite-proofreading enzyme". Herein, we report the molecular cloning and expression of this highly conserved enzyme of vancomycin-resistant Staphylococcus aureus (VRSA). Its functional and inhibition studies were performed for the first time by NMR spectroscopy. NMR studies showed the dehydration of S epimer of NADHX, in the presence of R-NADHX and cyc-NADHX, by NAD(P)H hydrate dehydratase. In addition, by employing the STD-NMR approach, a library of drugs and natural products (total 79) were evaluated for their binding interactions with the NAD(P)H hydrate dehydratase enzyme. Among them, seven compounds showed ligand-like interactions with the enzyme, and thus functional activity of the enzyme was again checked in the presence of each ligand. Compound 2 (Thiamine HCl) was found to fully inhibit the enzyme's function, and recognized as a potential inhibitor. Current study demonstrates that this enzyme deserves further studies as a potential drug target, as its inhibition can disrupt the normal metabolism of pathogenic VRSA.
Density Functional Studies of Coenzyme NADPH and Its Oxidized Form NADP++ : Structures, UV-Vis Spectra, and the Oxidation Mechanism of NADPH
J Comput Chem 2020 Feb 5;41(4):305-316.PMID:31713255DOI:10.1002/jcc.26103.
Density functional theory has been used to study the biologically important coenzyme NADPH and its oxidized form NADP++ . It was found that free NADPH prefers a compact structure in gas phase and exists in more extended geometries in aqueous solution. Ultraviolet-visible absorption spectra in aqueous solution were calculated for NADPH with an explicit treatment of 100 surrounding water molecules in combination with the COSMO solvation model for bulk hydration effects. The obtained spectra using the B3LYP hybrid density functional agree quite well with experimental data. The changes of Gibbs free energies ΔG in reactions of NADPH with O2 observed experimentally in cardiovascular and in chemical systems, that is, NADPH + 2 3 O2 → NADP++ + 2 O2- + H+ and NADPH + 1 O2 + H+ → NADP++ + H2 O2 , respectively, were calculated. The NADPH oxidation reaction in the cardiovascular system cannot proceed without activation since the obtained ΔG is positive. The reaction of NADPH in the chemical system with singlet oxygen was found to proceed in two ways, each consisting of two steps, that is, NADPH firstly reacts with 1 O2 barrierlessly to form NADP++ and HO2- , from which H2 O2 is formed in a spontaneous reaction with H+ , or 1 O2 and H+ initially form 1 HO2+ , which further reacts with NADPH to yield NADP++ and H2 O2 . © 2019 The Authors. Journal of Computational Chemistry published by Wiley Periodicals, Inc.
High-pressure protein crystal structure analysis of Escherichia coli dihydrofolate reductase complexed with folate and NADP+
Acta Crystallogr D Struct Biol 2018 Sep 1;74(Pt 9):895-905.PMID:30198899DOI:10.1107/S2059798318009397.
A high-pressure crystallographic study was conducted on Escherichia coli dihydrofolate reductase (ecDHFR) complexed with folate and NADP++ in crystal forms containing both the open and closed conformations of the M20 loop under high-pressure conditions of up to 800 MPa. At pressures between 270 and 500 MPa the crystal form containing the open conformation exhibited a phase transition from P21 to C2. Several structural changes in ecDHFR were observed at high pressure that were also accompanied by structural changes in the NADP++ cofactor and the hydration structure. In the crystal form with the closed conformation the M20 loop moved as the pressure changed, with accompanying conformational changes around the active site, including NADP++ and folate. These movements were consistent with the suggested hypothesis that movement of the M20 loop was necessary for ecDHFR to catalyze the reaction. In the crystal form with the open conformation the nicotinamide ring of the NADP++ cofactor undergoes a large flip as an intermediate step in the reaction, despite being in a crystalline state. Furthermore, observation of the water molecules between Arg57 and folate elucidated an early step in the substrate-binding pathway. These results demonstrate the possibility of using high-pressure protein crystallography as a method to capture high-energy substates or transient structures related to the protein reaction cycle.
Energetic basis on interactions between ferredoxin and ferredoxin NADP++ reductase at varying physiological conditions
Biochem Biophys Res Commun 2017 Jan 22;482(4):909-915.PMID:27894842DOI:10.1016/j.bbrc.2016.11.132.
In spite of a number of studies to characterize ferredoxin (Fd):ferredoxin NADP++ reductase (FNR) interactions at limited conditions, detailed energetic investigation on how these proteins interact under near physiological conditions and its linkage to FNR activity are still lacking. We herein performed systematic Fd:FNR binding thermodynamics using isothermal titration calorimetry (ITC) at distinct pH (6.0 and 8.0), NaCl concentrations (0-200 mM), and temperatures (19-28 °C) for mimicking physiological conditions in chloroplasts. Energetically unfavorable endothermic enthalpy changes were accompanied by Fd:FNR complexation at all conditions. This energetic cost was compensated by favorable entropy changes, balanced by conformational and hydrational entropy. Increases in the NaCl concentration and pH weakened interprotein affinity due to the less contribution of favorable entropy change regardless of energetic gains from enthalpy changes, suggesting that entropy drove complexation and modulated affinity. Effects of temperature on binding thermodynamics were much smaller than those of pH and NaCl. NaCl concentration and pH-dependent enthalpy and heat capacity changes provided clues for distinct binding modes. Moreover, decreases in the enthalpy level in the Hammond's postulate-based energy landscape implicated kinetic advantages for FNR activity. All these energetic interplays were comprehensively demonstrated by the driving force plot with the enthalpy-entropy compensation which may serve as an energetic buffer against outer stresses. We propose that high affinity at pH 6.0 may be beneficial for protection from proteolysis of Fd and FNR in rest states, and moderate affinity at pH 8.0 and proper NaCl concentrations with smaller endothermic enthalpy changes may contribute to increase FNR activity.