Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. Through the regulation of these ‘housekeeping’ metabolic networks, more effective anti-oxidation will be obtained by producing NADPH with concomitant expense of NADH (Fig. The third reaction is mediated by NADH kinase which directly phosphorylates NADH to form NADPH [48]. Nicotinamide adenine dinucleotide phosphate or NADPH is a reduced coenzyme that plays a key role in the synthesis of carbohydrates in photosynthetic organisms. However, recombinant NAD kinases expressed in E. coli are Ca2+/CaM independent. NAD is the reduced form of NAD+. Both NAD and NADP are structurally similar but, NADP contains a phosphate group. It creates the only obligate route for the de novo biosynthesis of NADP(H) in all living organisms. It also helps build nucleotides that end up as part of DNA and RNA. Nicotinamide Adenine Dinucleotide (NAD+) is a coenzyme present in biological systems. Function of NAD. However, NADP participates in defense against oxidative stress [44], and is a substrate for the synthesis of nicotinic acid adenine dinucleotide phosphate which is a potent intracellular Ca2+-mobilizing messenger. NADP+ differs from NAD+ by the presence of an additional phosphate group on the 2' position of the ribose ring that carries the adenine moiety. 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. Nicotinamide Adenine Dinucleotide (NAD) and Flavin Adenine Dinucleotide(FAD) are coenzymes involved in reversible oxidation and reduction reactions. “NADP+ phys” By NEUROtiker – Own work (Public Domain) via Commons Wikimedia, Lakna, a graduate in Molecular Biology & Biochemistry, is a Molecular Biologist and has a broad and keen interest in the discovery of nature related things, What is the Difference Between NAD+ and NADP+, What are the Similarities Between NAD+ and NADP+. 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]. 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. Then, these reduced coenzymes can donate these electrons to some other biochemical reaction normally involved in a process that is anabolic (like the sy… For the three NAD kinases of eukaryotic S. cerevisiae, Utr1p is inhibited by NADP+, NADH, and most strongly by NADPH [22]; Yef1p is weakly inhibited by NADH and NADPH [8]. Another inositol monophosphatase MJ0109 also has NADP phosphatase activity [53]. In human cells and in rats, NAD kinase controls NADPH concentration, which in turn influences the cellular anti-oxidative defense function [56,57]. A novel anti-oxidative defense strategies for converting NADH into NADPH inP. A1 [21], 33–35 kDa tetramer or dimer from M. tuberculosis [14,30,31], 34 kDa dimmer from M. flavus [14], and 37 kDa tetramer from archaeon P. horikoshii [19]. These three NAD kinase isozymes have different functions due to particular subcellular locations, with some functions weakly rescued by their isozymes [8,9]. Diphosphate group of the substrate played the role as a dication chelator, revealing a mechanism involving substrate-assisted catalysis. In glycolysis, glucose is converted to molecules of pyruvic acid. NADP+ is the used form of NADPH, and must be reduced with more electrons and a hydrogen. Accumulating evidence has suggested that NAD (including NAD+ and NADH) and NADP (including NADP+ and NADPH) could belong to the fundamental common mediators of various biological processes, including energy metabolism, mitochondrial functions, calcium homeostasis, antioxidation/generation of oxidative stress, gene expression, immunological functions, aging, and cell … Nicotinamide adenine dinucleotide. E. coli and Sphingomonas sp. [72] proposed NAD kinase as an interesting target for novel antibacterial drugs. For the two subsets of NADH and NAD+ kinases, the study of primary and tertiary structures demonstrated that phosphor acceptor specificity was determined by the second amino acid residue in the N-terminal upstream of the conserved domain II (Fig. 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]. NAD(H) is primarily involved in oxidative catabolic reactions, whereas NADP(H) participates in reductive anabolic reactions. 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. As green beans were subject to cold-shock, Ca2+/CaM-dependent NAD kinase activity was increased, which is closely related with proline metabolism, indicating their importance in cold acclimation of green bean plants [67]. S. cerevisiae [8,22,23] and E. gracilis [6]) are NTP-NAD kinases; human NAD kinase is ATP–NAD kinase [24]. Function od NADP. However, the main difference between NAD+ and NADP+ is the type of cellular metabolism. Studies showed that each subunit of M. tuberculosis NAD kinase consisted of an N-terminal α/β domain and a C-terminal 12-stranded β sandwich domain, connected by swapped β strands [31]. This work was supported by a grant from the National Natural Science Foundation of China (No. NAD+ refers to a coenzyme that occurs in many living cells and functions as an electron acceptor while NADP+ refers to a coenzyme that functions as a universal electron carrier, accepting electrons and hydrogen atoms to form NADPH or nicotinamide adenine dinucleotide phosphate. Nicotinamide adenine dinucleotide (NAD +) is essential not only for the harvesting of energy from substrates but also for an array of regulatory reactions that determine cellular health. [16]. It furthers the University's objective of excellence in research, scholarship, and education by publishing worldwide, This PDF is available to Subscribers Only. [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. Also, both work as electron carriers. NAD and NADP act as conezymes for many degydrogenases where they are involved in transfer of hydrogen, causing either oxidation or reduction of the substrates. As the most important coenzymes in living organisms, NAD(H) and NADP(H) participate in more than 300 different oxidative–reductive reactions [40], their importance in substance metabolism and energy metabolism has long been known. These results indicate that the phosphoryl donor specificity of NAD kinases depends on organisms [12] and may reflect organism's phylogeny. 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. Feng Shi, Yongfu Li, Ye Li, Xiaoyuan Wang, Molecular properties, functions, and potential applications of NAD kinases, Acta Biochimica et Biophysica Sinica, Volume 41, Issue 5, May 2009, Pages 352–361, https://doi.org/10.1093/abbs/gmp029. It exists in nearly all classes of living organisms and is proposed to be a primitive energy source that functions as an ATP substitute. Recently, NADP phosphatase has been found in several organisms. 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]. The Asp residue of GGDG motif in LmNADK1 activated the phosphor acceptor NAD+ and then made it accept the terminal phosphate residue of Mg2+–ATP to form NADP+ [36]. Although NAD kinase has a central role in the NAD(H)/NADP(H) metabolic network, especially in the one-step and cyclic supplying of NADPH, its regulatory mechanism has not been well elucidated. NADH is the reduced form of NAD+. NADH is the reduced state of NAD. Since thermo-stable poly(P)-dependent NAD kinase is more useful for enzymatic NADP(H) production, the hyperthermophilic archaea NAD kinases would have a higher application potential [19]. 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. The oligomeric assembly of NAD kinases may be due to their catalytic mechanism. In eubacterium E. coli, the 3′-phosphoadenosine 5′-phosphate phosphatase (CysQ) exhibits NADP phosphatase activity in vitro, but not in vivo [53]. 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. 1. Reaction mediated by pyridine nucleotide transhydrogenase transfers a hydride from NADH to NADP+ with the concurrent production of NADPH and NAD+. Based on the elucidation of gene or genomic information in numerous living organisms, the anti-oxidative function of NAD kinase has been proved. According to the phosphoryl acceptor of NAD kinases, some studies reported that NAD kinases from Gram-negative bacteria (e.g. They play a vital role in enzyme-catalyzed metabolic r… This is typically done during photosynthesis in plants, or as part of sugar digestion in animals. Also, both can exist in their reduced form as well, which release electrons to reduce the product, serving as a reducing agent. NAD kinase of hyperthermophilic eubacterium Thermotoga maritime was also folded into two distinct domains: the N-terminal α/β domain and the unique middle β-sandwich architecture [38]. For example, one of the three NAD kinase isozymes of A. thaliana, NADK2, was a chloroplast NAD kinase that can bind Ca2+/CaM [10]. For full access to this pdf, sign in to an existing account, or purchase an annual subscription. NADK1 is calmodulin (CaM) independent, and NADK2 is able to bind Ca2+/CaM, which seems to be plant specific [10,11]. Since then, detailed properties of NAD kinases and their genes have been studied. It is often stated that these compounds are electron carriers because they accept electrons (become reduced) during catabolic steps in the breakdown of organic molecules such as carbohydrates and lipids. NADPH. 5), and then measured their NAD kinase inhibitory activities. Example of a coenzyme. 3). NADPH is the reduced state of NADP. In the chloroplast of plants, NAD kinase plays a vital role in energy transduction [11,68]. Identical sequences are highlighted in color shade. NADP+/NADPH is the unsung hero of the cell’s cofactors. M. flavus, M. tuberculosis [14] and B. subtilis [17]) and hyperthermophilic archaea (e.g. NAD and NADP are relative coenzymes. Inhibition of lipogenesis and induction of apoptosis by valproic acid in prostate cancer cells via the C/EBPα/SREBP-1 pathway, Identification of HOXA10 target genes in human endometrial stromal cells by RNA-seq analysis, Epidermal growth factor receptor promotes tumor progression and contributes to gemcitabine resistance in osteosarcoma, Cardiovascular disease in patients with COVID-19: evidence from cardiovascular pathology to treatment, About Acta Biochimica et Biophysica Sinica, Catalytic and Structural Properties of NAD Kinases, Roles of NAD Kinases in NAD(H)/NADP(H) Metabolism, Roles of NAD Kinase in Anti-Oxidative System, Physiological Function of NAD Kinase in Plants, Potential Application of NAD Kinase in the Designing of Novel Antibacterial Drug, Receive exclusive offers and updates from Oxford Academic, An active supercomplex of NADPH dehydrogenase mediated cyclic electron flow around Photosystem I from the panicle chloroplast of, Identification of succinic semialdehyde reductases from, Role of mitochondrial NADH kinase and NADPH supply in the respiratory chain activity of. NAD kinase was first discovered by Kornberg from S. cerevisiae in 1950 [13], whereas the gene encoding the NAD kinase was identified by Kawai in Micrococcus flavus and M. tuberculosis H37Rv in 2000 [14]. Plant NAD kinases were brought into sight earlier than those of microorganisms mainly because of the possession of both CaM-independent and CaM-regulated NAD kinase isoforms in plants. 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]. Although mitochondrial NADP+-dependent isocitrate dehydrogenase IDPm has an important function in the control of mitochondrial redox balance and cellular defense against oxidative damage [45], it depends on the support of tricarboxylic acid cycle. Besides the remarkable differences in substrate specificity, obvious diversities in regulatory mode also exist among NAD kinases from different sources. 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. A1 [21]) and single-cellular eukaryotes (e.g. What are the Similarities Between NAD+ and NADP+      – Outline of Common features 4. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD and NADH (H for hydrogen) respectively. Describe glycolsis in terms of energy input, energy output, and net gain of ATP. Over 400 enzymes require the niacin coenzymes, NAD and NADP, mainly to accept or donate electrons for redox reactions (5). Also, each phosphate group links with a five-carbon, ribose sugar. [36] on Listeria monocytogenes NAD kinase showed that NAD kinase (LmNADK1) and PFKs used the central Asp of DDGDT motif differently. NADP+/NADPH is involved in building triglycerides, cholesterol and steroid molecules, which are important in cell membranes and hormones. The molecular size of subunit from eukaryotes varied widely, e.g. Therefore, they can obtain electrons released by oxidation reactions, serving as an oxidizing agent. “Nicotinamide Adenine Dinucleotide (NAD).” Kimball’s Biology Pages, 5 Aug. 2003, Available Here2. Therefore, NAD+ is involved in the redox reactions of cellular respiration including glycolysis, TCA cycle, and electron transport chain. The first reaction is catalyzed by NADP+-dependent dehydrogenases, such as isocitrate dehydrogenase (ICDH), glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconate dehydrogenase (6PGDH), malate enzyme, and glutamate dehydrogenase (GDH) [45,46]. 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. Increasing levels of NAD synthetase and NAD kinase of rice through dihydroflavonol-4 reductase could result in the increased level of NADP(H), conferring the prevention of induced cell death in plants caused by hydrogen peroxide and bacterial disease [66]. 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. Chloroplast NAD kinase was also essential for energy transduction through the xanthophyll cycle in photosynthesis [68]. The NADK1-deficient mutant exhibited sensitivity to γ-irradiation and paraquat-induced oxidative stress, indicating that NADK1 also has an important role in protecting plants against oxidative stress [69]. State Key Laboratory of Food Science and Technology. The NADPH first accepts the electrons and hydrogen when special enzymes transfer these particles to the molecule NADP+. As NADP(H) is the crucial coenzyme for many cellular processes in living organisms, such as NADPH-dependent reductive anabolic pathways, signal transduction, and anti-oxidative defense system, NAD kinase may be critical for the normal cellular functions. Roles are involved in: Energy metabolism, mitochondrial functions. Recently, studies on the survival strategies of Pseudomonas fluorescens in oxidative environment proved that NAD kinase was requisite for the controlling of NAD(H)/NADP(H) balance, especially the sufficient supply of NADPH, to adapt to environmental variance [50–52], suggesting the critical role of NAD kinase on adjusting NAD(H)/NADP(H) coenzyme in the metabolic networks. The release of energy from the bonds of sugar, or the input of energy from the sun, allows the cells of these organisms to bind hydrogen with two electrons to NADP+, creating NADPH which can move this energy, electrons, and hydrogen to … 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. As NAD kinase is an essential enzyme in bacteria and shows significant functional diversity with its human counterpart, it can be regarded as an attractive target for the development of selective antibacterial drugs [15]. The molecular size of subunit from prokaryotes was approximately 30–35 kDa, e.g. NAD also has other functions, e.g. “Figure 07 01 01ab” By CNX OpenStax (CC BY 4.0) via Commons Wikimedia    2. It acts as a coenzyme in redox reactions, as a donor of ADP-ribose groups in ADP-ribosylation reactions, as a precursor of the second messenger molecule cyclic ADP-ribose, as well as acting as a substrate for bacterial DNA ligases and a group of enzymes called sirtuins that use NAD+to remove acetyl groups from proteins. Multiple alignment of the primary structure of NAD kinases from several organisms  The amino acid sequences of NAD kinases from Gram-negative bacteria E. coli and S. enterica, Gram-positive bacteria M. tuberculosis, B. subtilis, L. monocytogenes and M. luteus, hyperthermophilic archaeon A. fulgidus, and eukaryote S. cerevisiae (all the three enzymes of Pos5p, Utr1p and Yef1p) are aligned. NAD and NADP are two co-enzymes. Thus, NAD kinase is required and crucial in either the quick one-step NADPH generator or the more effective cyclic NADPH generator. Nicotinamide adenine dinucleotide phosphate, abbreviated NADP+ or, in older notation, TPN, is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent. Living systems have evolved numerous one-step strategies for the genesis of NADPH (Fig. pentose phosphate enzyme systems), such as in the ocular lens [49]. NAD kinase is a critical enzyme for the regulation of NAD(H) and NADP(H) balance (Fig. Tyr158 of domain II, whereas the conserved GGDG loop formed hydrogen bonds with the pyrophosphate group of ATP and the 2′ phosphate group of NADP+ [39]. Hence, they are involved in redox reaction of the cells. NAD kinases from Gram-positive bacteria (e.g. More than 200 enzymes require these coenzymes for electron transfer in redox reactions. Moreover, NADP+ also accepts a hydrogen atom or in other words, a pair of electrons, during redox reactions. It is used by all forms of cellular life. This review will focus on the molecular properties, functions, and potential applications of NAD kinases. Meanwhile, the phosphoenolpyruvate carboxykinase (PEPCK) was downregulated, but the pyruvate kinase (PK) was upregulated and its activity was enhanced. Traps and transfers hydrogen ions and electrons in cell reactions. NAD and NADP appear to support distinct functions (Figure … As many NAD kinases are allosteric enzymes, the NAD(H) and NADP(H) balance might be directly regulated by NAD kinase. Living organisms derive most of their energy from redox reactions, which are processes involving the transfer of electrons. Here, accepting a proton represents accepting a pair of electrons. Three-dimensional structure of NAD kinases also showed that they are homooligomers. What is the Difference Between NAD and NADP? The transfer of electron is a main function of NAD. Although more studies on NAD kinases need to be done, their important properties, physiologic functions, and potential applications have been exhibited, which opens a wide field in the basic and applied studies. 3). For example, ATP–NAD kinase utilizes ATP as the sole phosphoryl donor for NAD(H) phosphorylation; NTP-NAD kinase uses ATP as well as some other nucleoside triphosphates such as GTP, CTP, UTP, and ITP; poly(P)/NTP-NAD kinase utilizes NTP as well as inorganic polyphosphates [poly(P)]. NAD+. It works as a reducing agent in lipid and nucleic acid synthesis. NADP. But NadG, one of the NAD kinases of S. typhimurium, is inhibited by quinolinate [5], whereas B. subtilis NAD kinase is activated by quinolinate [17]. 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. 1). 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. The main types of anabolic reaction which uses NADP+ as an oxidizing agent are the Calvin cycle, the dark reaction of photosynthesis. Hence, this is another difference between NAD+ and NADP+. 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. NADPH is the reduced form of NADP+. Furthermore, NAD+ serves as a coenzyme in cellular respiration while NADP+ serves as a coenzyme in photosynthesis. Oxford University Press is a department of the University of Oxford. For hydrogen ) respectively reaction is mediated by pyridine nucleotide transhydrogenase transfers hydride. 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