But, NADP+ is reduced in the light reaction of photosynthesis and the reducing power of NADPH is used to assimilate carbon dioxide in the dark reaction. These enzymes had a common fold and a conserved GGDGT motif, and also a common strategy for catalysis. 4 Since its discovery, NAD + and its reduced form NADH, as well as NADP + and NADPH, have been well studied as coenzymes for many redox reactions. Function of NAD. [30,31] studied on M. tuberculosis NAD kinase, including its catalytic property and stereo structure, and attempted to design an effective enzyme inhibitor that could be used as a novel anti-tubercular drug for the treatment of re-emerging tuberculosis. Several lines of evidence presented here confirm the importance of IDH to respiratory processes. More than 200 enzymes require these coenzymes for electron transfer in redox reactions. For example, recombinant A. thaliana NAD kinases (NADK1, NADK2, and NADK3) could not be activated by Ca2+/CaM, even though recombinant NADK2 with a Ca2+-dependent CaM-binding motif in its N-terminal was able to bind CaM [10,11]. In yeast Schizosaccharomyces pombe, four NAD kinase homolog genes were presented [12]. Because poly(P) is a much less expensive phosphoryl donor than ATP or any other triphosphonucleotide, Poly(P)/NTP-NAD kinase should have potential application values. NAD+ is reduced to NADH in both glycolysis and TCA cycle, and the reducing power of NADH is used to generate ATP in the electron transport chain. The growing environment and physiologic status of different organisms, as well as the consequent cellular form and level of cofactors, may also lead to the divergence of regulatory mode of NAD kinases, especially when several NAD kinase isozymes are presented. Significantly, the structural components of NADP are the same as NAD. State Key Laboratory of Food Science and Technology. NAD kinase catalyzes the phosphorylation of NAD(H) to form NADP(H), using ATP as phosphoryl donor. NAD(H) is primarily involved in oxidative catabolic reactions, whereas NADP(H) participates in reductive anabolic reactions. Read "Amino acid residues that determine functional specificity of NADP‐ and NAD‐dependent isocitrate and isopropylmalate dehydrogenases, Proteins: Structure Function and Bioinformatics" on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips. The molecular size of subunit from eukaryotes varied widely, e.g. Thus, this is the main difference between NAD+ and NADP+. Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Generally, NAD has two phosphate groups linked by an oxygen molecule. The ability to construct certain molecules allows organisms to control their cellular growth and division. Moreover, they are a form of nicotinamide-adenine nucleotides. 4). Most biochemical reactions require protein catalysts (enzymes). Home » Science » Chemistry » Biochemistry » What is the Difference Between NAD+ and NADP+. Owing to these significant and distinguishable function of NAD(H) and NADP(H), their metabolism and intracellular balance must be tightly regulated. Moreover, NADP+ also accepts a hydrogen atom or in other words, a pair of electrons, during redox reactions. CaM is a major intracellular calcium receptor in both animal and plant cells, it undergoes conformational change upon binding calcium and then interacts with a variety of target enzymes to modulate their activities [63]. fluorescens(modified from Singhet al.50)  MDH, malate dehydrogenase; NADK, NAD kinase; ME, malic enzyme; PC, pyruvate carboxylase; PEPCK, phosphoenolpyruvate carboxykinase; PK, pyruvate kinase; ICL, isocitrate lyase; MS, malate synthase. As a crucial enzyme, the essentiality of NAD kinase has been demonstrated in several microorganisms, such as B. subtilis [2], M. tuberculosis [1], E. coli [3], S. enterica [4], Streptococcus pneumoniae [70], Staphylococcus aureus [71], Pseudomonas aeruginosa [36], and S. cerevisiae [7]. Although the mechanisms regulating NAD(H)/NADP(H) metabolic flux are not fully elucidated, the significance of NAD kinase has been well accepted, especially the central role of NAD kinase in NADPH supplying network. This work was supported by a grant from the National Natural Science Foundation of China (No. Search for other works by this author on: Genes required for mycobacterial growth defined by high-density mutagenesis, From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways, Evidence that feedback inhibition of NAD kinase controls responses to oxidative stress, Evidence for the existence of two soluble NAD, Synthetic lethal and biochemical analyses of NAD and NADH kinases in, Identification of ATP-NADH kinase isozymes and their contribution to supply of NADP(H) in, Cloning and characterization of two NAD kinases from, Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H), Enzymatic synthesis of triphosphopyridine nucleotide, Inorganic polyphosphate/ATP-NAD kinase of, Structural and functional properties of NAD kinase, a key enzyme in NADP biosynthesis, Metaphosphate: a new phosphoryl donor for NAD phosphorylation, First archaeal inorganic polyphosphate/ ATP-dependent NAD kinase, from hyperthermophilic archaeon, Overexpression, purification, and characterization of ATP-NAD kinase of, A novel NADH kinase is the mitochondrial source of NADPH in, Structural and functional characterization of human NAD kinase, Inorganic polyphosphate: a molecule of many functions, Establishment of a mass-production system for NADP using bacterial inorganic polyphosphate/ATP-NAD kinase, Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution, Pigeon-liver NAD kinase. As NAD kinase is a crucial enzyme that regulates the levels of NAD(H)/NADP(H) in the metabolic pathways, enzymatic properties of NAD kinases from several organisms have been studied in the past decade. NAD+ kinase (EC 2.7.1.23) only phosphorylates NAD+ to form NADP+; NADH kinase (EC 2.7.1.86) phosphorylates both NAD+ and NADH to form NADP+ and NADPH. Too much NADH can lead to the release of Fe2+ to accumulate reactive oxygen species by respiratory chain or oxidases, suggesting NADH could be a pro-oxidant [5,59]. For example, two NAD kinases, NadF and NadG, were found in Salmonella typhimurium [5]; two NAD kinases isozymes with distinctive catalytic mechanisms and Km values were presented in Euglena gracilis [6]. The molecular size of subunit from prokaryotes was approximately 30–35 kDa, e.g. Several lines of evidence presented here confirm the importance of IDH to respiratory processes. NADP+/NADPH is involved in building triglycerides, cholesterol and steroid molecules, which are important in cell membranes and hormones. It is also a universal cofactor for numerous enzymes participating in detoxification reactions, including glutathione reductase [58], thioredoxin reductase and cytochrome P450 reductase. Three NAD kinases, NADK1, NADK2, and NADK3, were also found in Arabidopsis thaliana. One nucleotide contains an adenine nucleobase and the other nicotinamide. As in vitro regulatory patterns of NAD kinases differ distinctively among microbes, the control of enzymatic activity, particularly through allosteric regulation, as well as the regulatory mechanism of NAD kinase to the NAD(H)/NADP(H) metabolic flux has not been elucidated. Compounds 1 and 2 could inhibit human NAD kinase, whereas compound 3 could inhibit both the human and M. tuberculosis NAD kinase, and BAD was the most potent competitive inhibitor of the human NAD kinase [73]. 2). 30 kDa hexamer from E. coli [20], 32 kDa dimmer from Sphingomonas sp. Although it has been proved that NAD kinases from all living organisms are highly conserved, differences in the enzymatic properties from various organisms may exist. Further more, the enhanced activity of isocitrate lyase (ICL) and malate synthase (MS) of glyoxylate cycle could promote the supplying of malate, which in turn could contribute to NADP+ reduction. It is used by all forms of cellular life. CaM-dependent NAD kinase could play a metabolic role and participate in Ca2+-mediated cellular defense against invading pathogens in plants by helping to provide reductant for the NADPH-dependent oxidative burst [65]. [36] on Listeria monocytogenes NAD kinase showed that NAD kinase (LmNADK1) and PFKs used the central Asp of DDGDT motif differently. However, the main structural difference between NADP and NAD is the presence of an additional phosphate group in the NADP on the 2′ carbon of the ribose ring, which links to the adenine moiety. The supply of NADPH in living systems can be fulfilled through several one-step enzymatic reactions (Fig. E. coli [20] and Sphingomonas sp. NADP+/NADPH is the unsung hero of the cell’s cofactors. Nicotinamide adenine dinucleotide (NAD) is a cofactor central to metabolism. It exists in nearly all classes of living organisms and is proposed to be a primitive energy source that functions as an ATP substitute. Published by ABBS Editorial Office in association with Oxford University Press on behalf of the Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences. However, the molecular size of subunit from the archaeon M. jannaschii was much larger as 64 kDa, since two distinguishable regions of NAD kinase and NADP phosphatase existed [18], and the sequence showed a low level of identity to those of E. coli (31%) and of M. tuberculosis (29%) [18]. Three conserved sequences of GGDG motif, NE/D short motif and conserved domain II are specified in box. Conversion and regeneration pathway of coenzyme NAD+/NADH and NADP+/NADPH  Reactions catalyzed by NAD+ kinase, NADP phosphatase and NADH kinase are responsible for the conversion between NAD(H) and NADP(H). [73] have synthesized several novel analogs of NAD+, that is, the C2' hydroxyl group of the adenosine ribose replaced by fluorine in the ribo configuration giving compound 1, in the arabino configuration giving compound 2, the C2' hydroxyl group inverted into arabino configuration giving compound 3, and an uncharged benzamide adenine dinucleotide (BAD) (Fig. However, the application of NAD kinase in cofactor engineering has not been reported. “Nicotinamide Adenine Dinucleotide (NAD).” Kimball’s Biology Pages, 5 Aug. 2003, Available Here2. NADP+ functions alongside many enzymes to provide energy to the many reactions in a cell. Here only the oxidized form of NAD(P)+ is shown. NADPH is synthesized by the light reaction of photosynthesis and its reduction power is used in the dark reaction in order to assimilate carbon dioxide. NAD and NADP are two co-enzymes. The precursors of NAD+ biosynthesis, such as quinolinate and nicotinic acid, do not influence NAD kinase activity in general. The study by Labesse et al. proteins. The third reaction is mediated by NADH kinase which directly phosphorylates NADH to form NADPH [48]. Another inositol monophosphatase MJ0109 also has NADP phosphatase activity [53]. The most important function of NAD are these electron transferring reactions. To realize the reasons for the differences of catalytic properties, conserved sequences and active center residues of some NAD kinases were analyzed recently [34]. Over 400 enzymes require the niacin coenzymes, NAD and NADP, mainly to accept or donate electrons for redox reactions (5). These differences might be due to the properties of the host expression system [12]. Function od NADP. NADPH is vital in intracellular anti-oxidative defense system for most organisms, and its central role in the resistance of oxidative stress has been proved [51]. At the same time, NAD kinase (NADK), malic enzyme (ME), together with pyruvate carboxylase (PC) of gluconeogenesis, and malate dehydrogenase (MDH) of tricarboxylic acid cycle were upregulated, ensuring the cyclic supplying of NADPH from NADH. NAD and NADP are relative coenzymes. Different from NAD(H) phosphorylation, the reverse process of NADP(H) dephosphorylation has not been well studied, although it might influence the NAD(H)/NADP(H) metabolism and balance. However, as these one-step reactions cannot be performed circularly, they are not so effective while operated separately. In addition to the metabolic function, both NADH and NADPH have important physiological functions including gene expression, mitochondrial functions, calcium regulation, antioxidation and the generation of oxidative stress, immune functions, the aging process, and cell death. Several studies have indicated that NAD kinase is essential for the survival of certain organisms, such as Mycobacterium tuberculosis [1], Bacillus subtilis [2], Escherichia coli [3], and Salmonella enterica [4]. Reduced nicotinamide adenine dinucleotide phosphate (NADPH) is an essential electron donor in all eukaryotes, bacteria, and archaea. Homolog genes of NAD kinase can be found in all the sequenced genomes of living organisms, including prokaryotes and eukaryotes, with the exception of the intracellular parasite Chlamydia trachomatis [4]. However, continuous supply of NADPH depends on the cyclic metabolic networks. This would be helpful for exploiting novel antimicrobial drugs. Both NAD and NADP are structurally similar but, NADP contains a phosphate group. After the addition of 1.0 ml of ethanol, the mixture was exposed to a stream of air at 25 °C until dry, then dissolved again in 1.0 ml of water. NAD+ is the oxidized form of NAD (nicotinamide adenine dinucleotide), which is a coenzyme involved in catabolic reactions as an electron carrier. For example, when P. fluorescens was exposed to oxidative stress triggered by menadione insult, some enzymes involved in disparate metabolic modules could converge to create a metabolic network in order to convert NADH into NADPH. Nicotinamide Adenine Dinucleotide (NAD+) is a coenzyme present in biological systems. Such studies showed that purified NAD kinases from some organisms were indeed regulated in vitro by effectors such as NAD(H) or NADP(H), but difference in the regulatory mode existed. Furthermore, one ribose sugar links with an adenine nucleotide while the second ribose sugar links with a nicotinamide moiety. However, up to date, no effective inhibitors have been developed that only suppress bacterial and fungi NAD kinases but not humans. In general, NAD takes part in the catabolic reactions, which NADP in synthetic pathway reactions. Identical sequences are highlighted in color shade. For example, in S. enterica [4] and in the mitochondria of S. cerevisiae [7,8,23,55], NAD kinase plays a major role in protecting living cells against oxidative stress. Therefore, NAD+ kinase or NADH kinase activity is required for sustaining the NADPH level to regenerate the anti-oxidative system. In addition, NADP is involved in the pentose phosphate pathway in animals as a coenzyme. However, the main difference between NAD+ and NADP+ is the type of cellular metabolism. Differences in catalytic properties and molecular structure also exist between microbial and human NAD kinases, such as phosphoryl donor specificity and molecular size of subunit. Although the physiologic functions, influence pathways, and regulatory mechanisms of NAD kinases have not been clearly elucidated, some of their characteristics, functions, and potential applications have been revealed. NAD and NADP appear to support distinct functions (Figure … NADP+ is the used form of NADPH, and must be reduced with more electrons and a hydrogen. For the NAD kinase of hyperthermophilic archaeon Archaeoglobus fulgidus, the AMP portion of substrate ATP molecule used the same binding site as the nicotinamide ribose portion of product NADP+, i.e. Recent studies have partially demonstrated that NAD kinase plays a crucial role in the regulation of NAD(H)/NADP(H) conversion. NAD acts as cofactor in redox reactions. 3). Thi… During the interaction, the electrons change NADP from its oxidized state - NADP + - to its reduced state - NADPH. 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