| Customization: | Available |
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| CAS No.: | 53-84-9 |
| Formula: | C21h27n7o14p2 |
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When bound in the active site of an oxidoreductase, the nicotinamide ring of the coenzyme is positioned so that it can accept a hydride from the other substrate. Depending on the enzyme, the hydride donor is positioned either "above" or "below" the plane of the planar C4 carbon, as defined in the figure. Class A oxidoreductases transfer the atom from above; class B enzymes transfer it from below. Since the C4 carbon that accepts the hydrogen is prochiral, this can be exploited in enzyme kinetics to give information about the enzyme's mechanism. This is done by mixing an enzyme with a substrate that has deu* atoms substituted for the hydrogens, so the enzyme will reduce NAD+ by transferring deu* rather than hydrogen. In this case, an enzyme can produce one of two stereoisomers of NADH.
Despite the similarity in how proteins bind the two coenzymes, enzymes almost always show a high level of specificity for either NAD+ or NADP+. This specificity reflects the distinct metabolic roles of the respective coenzymes, and is the result of distinct sets of amino acid residues in the two types of coenzyme-binding pocket. For instance, in the active site of NADP-dependent enzymes, an ionic bond is formed between a basic amino acid side-chain and the acidic phosphate group of NADP+. On the converse, in NAD-dependent enzymes the charge in this pocket is reversed, preventing NADP+ from binding. However, there are a few exceptions to this general rule, and enzymes such as aldose reductase, glucose-6-phosphate dehydrogenase, and methylenetetrahydrofolate reductase can use both coenzymes in some species.
Nicotinamide adenine dinucleotide (NAD+) is a coenzyme for redox reactions, making it central to energy metabolism. NAD+ is also an essential cofactor for non-redox NAD+-dependent enzymes, including sirtuins, CD38 and poly(ADP-ribose) polymerases. NAD+ can directly and indirectly influence many key cellular functions, including metabolic pathways, DNA repair, chromatin remodelling, cellular senescence and immune cell function. These cellular processes and functions are critical for maintaining tissue and metabolic homeostasis and for healthy ageing. Remarkably, ageing is accompanied by a gradual decline in tissue and cellular NAD+ levels in multiple model organisms, including rodents and humans. This decline in NAD+ levels is linked causally to numerous ageing-associated diseases, including cognitive decline, cancer, metabolic disease, sarcopenia and frailty. Many of these ageing-associated diseases can be slowed down and even reversed by restoring NAD+ levels. Therefore, targeting NAD+ metabolism has emerged as a potential therapeutic approach to ameliorate ageing-related disease, and extend the human healthspan and lifespan. However, much remains to be learnt about how NAD+ influences human health and ageing biology
NAD is useful for various life processes which are responsible for the proper maintenance and functioning of the body. Basically, it is used to generate energy in the body and to guard against many diseases.
1. Nicotinamide adenine dinucleotide (NAD) for Skincare: Being the highest coenzyme in metabolic process and the ability to repair damaged cells make NAD the most potent antioxidant. It helps in reducing the signs of aging and works as an essential element in skin care and provides energy to the aged and dead cells.
2. NAD in Cellular Respiration: NAD is an important enzyme in generating (Adenosine triphosphate) ATP which is the most important part of cellular respiration. Every cell in the body needs thousands of units of ATP and Nicotinamide adenine dinucleotide(NAD) helps in attaining this resource for the cells.
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Function 1. NADH is used for improving mental clarity, alertness, concentration, and memory; as well as for treating Alzheimer's disease and dementia. Because of its role in energy production, NADH is also used for improving athletic performance and treating chronic fatigue syndrome. |
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Application 1. Diagnostic reagents raw materials, scientific research experiments. |
* The statements in this section have not been evaluated by the FDA or EFSA.
References
1.Xue X, et al. FEBS Lett. 2023. PMID: 36310388
2.Arenas-Jal M, et al. Eur J Pharmacol. 2020. PMID: 32360833 Review.
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