NADP+
(Synonyms: 烟酰胺腺嘌呤双核苷酸磷酸盐,Coenzyme II, β-NADP, Nicotinamide adenine dinucleotide phosphate, TPN) 目录号 : GC44307
The oxidized form of NADPH
Cas No.:53-59-8
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
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- Purity: >98.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
NADP+ is the oxidized form of the electron donor nicotinamide adenine dinucleotide phosphate. NADP+ together with its reduced form, reduced NADPH, is involved in maintaining redox balance and supporting the biosynthesis of fatty acids and nucleic acids [1].
NADP+, a structural analogue of NAD+, is synthesized by transferring a phosphate group from ATP to the 2′-hydroxyl group of the adenosine ribose moiety of NAD+. This reaction is catalyzed by NADKs [2]. NADP+ act as a cofactor in various biological reactions [3]. NADP+/NADPH is important in regulating the cellular redox state, energy metabolism, mitochondrial function, gene expression, and signaling pathways, NADP+/NADPH are essential for maintaining a large array of biological processes[3,4,5].
References:
[1]. Yang, Yue, and Anthony A. Sauve. "NAD+ metabolism: Bioenergetics, signaling and manipulation for therapy." Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics 1864.12 (2016): 1787-1800.
[2]. Ying, Weihai. "NAD+/NADH and NADP+/NADPH in cellular functions and cell death: regulation and biological consequences." Antioxidants & redox signaling 10.2 (2008): 179-206.
[3]. Jackson J B. A review of the binding-change mechanism for proton-translocating transhydrogenase[J]. Biochimica et Biophysica Acta (BBA)-Bioenergetics, 2012, 1817(10): 1839-1846.
[4]. Cantó, Carles, and Johan Auwerx. "NAD+ as a signaling molecule modulating metabolism." Cold Spring Harbor symposia on quantitative biology. Vol. 76. Cold Spring Harbor Laboratory Press, 2011.
[5]. Cantó, Carles, Keir J. Menzies, and Johan Auwerx. "NAD+ metabolism and the control of energy homeostasis: a balancing act between mitochondria and the nucleus." Cell metabolism 22.1 (2015): 31-53.
NADP+ 是电子供体烟酰胺腺嘌呤二核苷酸磷酸的氧化形式。 NADP+ 及其还原型 NADPH 参与维持氧化还原平衡并支持脂肪酸和核酸的生物合成[1]。
NADP+ 是 NAD+ 的结构类似物，通过将磷酸基团从 ATP 转移到 NAD+ 的腺苷核糖部分的 2'-羟基而合成。该反应由 NADKs [2] 催化。 NADP+ 在多种生物反应中作为辅助因子[3]。 NADP+/NADPH在调节细胞氧化还原状态、能量代谢、线粒体功能、基因表达和信号通路方面具有重要作用，NADP+/NADPH对维持大量生物过程至关重要[3,4,5].
| Cas No. | 53-59-8 | SDF | |
| 别名 | 烟酰胺腺嘌呤双核苷酸磷酸盐,Coenzyme II, β-NADP, Nicotinamide adenine dinucleotide phosphate, TPN | ||
| 化学名 | adenosine 5'-(trihydrogen diphosphate), 2'-(dihydrogen phosphate), P'→5'-ester with 3-(aminocarbonyl)-1-β-D-ribofuranosylpyridinium, inner salt | ||
| 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 | 分子量 | 743.4 |
| 溶解度 | Soluble in PBS, PH7.2, 10mg/mL | 储存条件 | Store at -20°C,protect from light |
| 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。
In cancer, all roads lead to NADPH
Pharmacol Ther 2021 Oct;226:107864.PMID:33894275DOI:10.1016/j.pharmthera.2021.107864.
Cancer cells require increased levels of NADPH for increased nucleotide synthesis and for protection from ROS. Recent studies show that increased NADPH is generated in several ways. Activated AKT phosphorylates NAD kinase (NADK), increasing its activity. NADP+ formed, is rapidly converted to NADPH by glucose 6-phosphate dehydrogenase and malic enzymes, overexpressed in tumor cells with mutant p53. Calmodulin, overexpressed in some cancers, also increases NADK activity. Also, in IDH1/2 mutant cancer, NADPH serves as the cofactor to generate D-2 hydroxyglutarate, an oncometabolite. The requirement of cancer cells for elevated levels of NADPH provides an opportunity to target its synthesis for cancer treatment.
NADPH production by the oxidative pentose-phosphate pathway supports folate metabolism
Nat Metab 2019 Mar;1:404-415.PMID:31058257doi
NADPH donates high energy electrons for antioxidant defense and reductive biosynthesis. Cytosolic NADP+ is recycled to NADPH by the oxidative pentose phosphate pathway (oxPPP), malic enzyme 1 (ME1) and isocitrate dehydrogenase 1 (IDH1). Here we show that any one of these routes can support cell growth, but the oxPPP is uniquely required to maintain a normal NADPH/NADP+ ratio, mammalian dihydrofolate reductase (DHFR) activity and folate metabolism. These findings are based on CRISPR deletions of glucose-6-phosphate dehydrogenase (G6PD, the committed oxPPP enzyme), ME1, IDH1, and combinations thereof in HCT116 colon cancer cells. Loss of G6PD results in high NADP+, which induces compensatory increases in ME1 and IDH1 flux. But the high NADP+ inhibits dihydrofolate reductase (DHFR), resulting in impaired folate-mediated biosynthesis, which is reversed by recombinant expression of E. coli DHFR. Across different cancer cell lines, G6PD deletion produced consistent changes in folate-related metabolites, suggesting a general requirement for the oxPPP to support folate metabolism.
NADP-dependent enzymes. I: Conserved stereochemistry of cofactor binding
Proteins 1997 May;28(1):10-28.PMID:9144787DOI:10.1002/(sici)1097-0134(199705)28:1<10::aid-prot2>3.0.co;2-n.
The ubiquitous redox cofactors nicotinamide adenine dinucleotides [NAD and NADP+] are very similar molecules, despite their participation in substantially different biochemical processes. NADP+ differs from NAD in only the presence of an additional phosphate group esterified to the 2'-hydroxyl group of the ribose at the adenine end and yet NADP+ is confined with few exceptions to the reactions of reductive biosynthesis, whereas NAD is used almost exclusively in oxidative degradations. The discrimination between NAD and NADP+ is therefore an impressive example of the power of molecular recognition by proteins. The many known tertiary structures of NADP+ complexes affords the possibility for an analysis of their discrimination. A systematic analysis of several crystal structures of NAD(P)-protein complexes show that: 1) the NADP+ coenzymes are more flexible in conformation than those of NAD; 2) although the protein-cofactor interactions are largely conserved in the NAD complexes, they are quite variable in those of NADP+; and 3) in both cases the pocket around the nicotinamide moiety is substrate dependent. The conserved and variable interactions between protein and cofactors in the respective binding pockets are reported in detail. Discrimination between NAD and NADP+ is essentially a consequence of the overall pocket and not of a few residues. A clear fingerprint in NAD complexes is a carboxylate side chain that chelates the diol group at the ribose near the adenine, whereas in NADP+ complexes an arginine side chain faces the adenine plane and interacts with the phosphomonoester. The latter type of interaction might be a general feature of recognition of nucleotides by proteins. Other features such as strand-like hydrogen bonding between the NADP+ diphosphate moieties and the protein are also significant. The NADP+ binding pocket properties should prove useful in protein engineering and design.
Identification of the NADP++ Structural Binding Site and Coenzyme Effect on the Fused G6PD::6PGL Protein from Giardia lamblia
Biomolecules 2019 Dec 27;10(1):46.PMID:31892224DOI:10.3390/biom10010046.
Giardia lambia is a flagellated protozoan parasite that lives in the small intestine and is the causal agent of giardiasis. It has been reported that G. lamblia exhibits glucose-6-phosphate dehydrogenase (G6PD), the first enzyme in the pentose phosphate pathway (PPP). Our group work demonstrated that the g6pd and 6pgl genes are present in the open frame that gives rise to the fused G6PD::6PGL protein; where the G6PD region is similar to the 3D structure of G6PD in Homo sapiens. The objective of the present work was to show the presence of the structural NADP++ binding site on the fused G6PD::6PGL protein and evaluate the effect of the NADP++ molecule on protein stability using biochemical and computational analysis. A protective effect was observed on the thermal inactivation, thermal stability, and trypsin digestions assays when the protein was incubated with NADP++. By molecular docking, we determined the possible structural-NADP+ binding site, which is located between the Rossmann fold of G6PD and 6PGL. Finally, molecular dynamic (MD) simulation was used to test the stability of this complex; it was determined that the presence of both NADP++ structural and cofactor increased the stability of the enzyme, which is in agreement with our experimental results.
Caged NADP+ and NAD. Synthesis and characterization of functionally distinct caged compounds
Biochemistry 1997 Jul 22;36(29):9035-44.PMID:9220992DOI:10.1021/bi970263e.
Two caged NADP+ compounds have been synthesized and characterized for use in the crystallographic study of isocitrate dehydrogenase (IDH), as well as for general use in cell biology, metabolism, and enzymology. One caged NADP+ compound has been designed to be "catalytically caged" so that it can bind to IDH prior to photolysis but is not catalytically active. A second NADP+ compound is "affinity caged" so that addition of the caging group inhibits binding of the compound to IDH prior to photolysis. The catalytically caged compound was synthesized in a two-step process, starting with the NADase-catalyzed exchange of a synthetic nicotinamide derivative onto NADP+. X-ray structures of the NADP+ compounds with IDH show the catalytically caged NADP+ bound to the enzyme with its nicotinamide group improperly positioned to allow turnover, while the affinity caged NADP+ does not bind to the enzyme at concentrations up to 50 mM. Two analogous caged NAD compounds have also been synthesized. The NADP+ and NAD compounds were characterized in terms of kinetics, quantum yield, and product formation. The affinity caged NADP+ compound P2'-[1-(4,5-dimethoxy-2-nitrophenyl)ethyl] NADP+ (VIII) is photolyzed at a rate of 1.8 x 10(4) s-1 with a quantum yield of 0.19 at pH 7; the NAD analog P-[1-(4,5-dimethoxy-2-nitrophenyl)ethyl] NAD (IX) is photolyzed at at a rate of 1.7 x 10(4) s-1 with a quantum yield of 0.17.