NAD+

NAD+ is an important coenzyme in the oxidation-reduction reactions of the human body and appears in many metabolic reactions in cells. As an indispensable cofactor for biochemical catalytic reactions, it participates in over a thousand physiological reactions, such as the tricarboxylic acid (TCA) cycle and beta-oxidation of fat, and plays an important role in the metabolic utilization of nutrients such as sugar, fat, and amino acids. It is also the sole substrate for NAD+-consuming enzymes (such as NAD+-dependent ADP ribosyltransferases). These enzymes use NAD+ as a substrate to break it down into ADP ribose and nicotinamide (Nam), and they play different physiological roles in different cells, such as participating in DNA repair and regulating cellular oxidative stress.

Initially, the physiological function of NAD+ was focused on cellular metabolism of substances and energy. It serves as an essential cofactor for biological catalytic reactions, participating in over a thousand physiological reactions, such as the tricarboxylic acid (TCA) cycle and beta-oxidation of fat, etc. It has significant meaning in the metabolic utilization of nutrients such as sugar, fat, and amino acids. Especially in mitochondria, NAD+ accepts electron transfer and is reduced to reduced coenzyme I (NADH) in the TCA cycle. Through electron transfer, it can inhibit the generation of free radicals, increase glutathione content, inhibit the release of cytochrome C from mitochondria, and at the same time, as the most important hydrogen donor in the electron transfer chain, 1 mol of coenzyme I (NAD) can generate 3 mol of ATP, which is an important source of energy for cellular life activities. In addition, NAD+ metabolites such as coenzyme II (NADP(H)), nicotinamide (NAM), ADP ribose, etc. play important roles in human cell energy metabolism, oxidative stress regulation, and signal pathway transmission. The content of coenzyme I in high-energy-consuming tissues such as the heart, brain, and muscle is significantly higher than that in other tissues.

NAD is a coenzyme of dehydrogenases, such as ethanol dehydrogenase (ADH), used to oxidize ethanol. It plays an irreplaceable role in glycolysis, gluconeogenesis, tricarboxylic acid cycle and respiratory chain. The intermediate will pass the removed hydrogen to NAD, making it NADH + H.
NADH + H, on the other hand, acts as a carrier of hydrogen and syntheses ATP through chemiosmotic coupling in the electron transport chain.
In terms of light absorption, NADH has an absorption peak at 260nm and 340nm, while NAD+ only has an absorption peak at 260nm, which is an important attribute that distinguishes the two. This is also the physical basis for measuring metabolic rate in many metabolic tests. NAD has a light absorption coefficient of 1.78*10L /(mol*cm) at 260nm, while NADH has a light absorption coefficient of 6.2*10³ L/(mol*cm) at 340nm.

Coenzyme I (NAD), chemically called nicotinamide adenine dicriboglycine or nicotinoside diphosphate, exists in the oxidized (NAD+) and reduced (NADH) states in mammals, and is an important coenzyme in human REDOX reactions. At the same time, it is the only substrate for Coenzyme I-consuming enzymes (such as NAD+ dependent ADP ribosyltransferase), which can only facilitate the breakdown of Coenzyme I (NAD+) as a substrate into ADP ribose and niacinamide (Nam), which perform different physiological functions in different cells. There are three main types of these enzymes in the body:
1.ADP ribosyltransferase or polyribosylpolymerase (PARP) :
These enzymes are involved in DNA repair, gene expression, cell cycle progression, cell survival, chromosome reconstruction and gene stability.
2. Cyclic ADP ribose synthases (cADPR synthases) Cyclic ribose polymerase (cADP synthases) :
It is composed of a pair of extracellular enzymes, called lymphocyte antigens CD38 and CD157, which use NAD as a substrate to generate cyclic ADP ribose (an important calcium signaling messenger), which is important in calcium homeostasis maintenance and immune response.
3, Ⅲ protein lysine deacetylase Sirtuins:
They are a class of histone deacetylases with seven different subtypes (SIRT1-SIRT7) that play an important role in cell stress resistance, energy metabolism, apoptosis, and aging. A large number of studies have shown that the regulation of metabolic balance by Sirtuins will directly affect various diseases related to metabolism. For example, SIRT1 regulates the acetylation state of histones with the participation of Coenzyme I(NAD), and plays an important role in enhancing cardiac tolerance to oxidative stress, regulating myocardial energy metabolism and anti-aging.

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In recent years, it has been found that as the only substrate of Coenzyme I consuming enzyme (NAD+ dependent ADP ribosyl transferase), it participates in the generation of signal molecules and participates in many physiological functions. There are three main types of these enzymes in the body: 1.ADP ribosyl transferase or polyribosyl polymerase (PARP); 2. Cyclic ADP ribose synthases (cADPR synthases); 3.III protein lysine deacetylase sirtuins. These enzymes decompose Coenzyme I (NAD+) as a substrate into ADP ribose and niacinamide (Nam), which play different physiological functions in different cells. For example, PARP is located in the nucleus of a variety of cells, when free radicals and oxidants cause damage to the cell, the single strand of DNA will be broken, and PARP will be activated. Activated PARP uses Coenzyme I(NAD+) as a substrate to transfer ADP ribosyl to target proteins while generating niacinamide (Nam), which are involved in a variety of functions such as DNA repair, gene expression, cell cycle progression, cell survival, chromosome reconstruction, and gene stability. Cyclic ribose polymerase (cADP synthase) is composed of a pair of extracellular enzymes, the familiar lymphocyte antigens CD38 and CD157, that use NAD as a substrate to produce cyclic ADP ribose, an important calcium signaling messenger. It has important physiological significance in the maintenance of calcium homeostasis and immune response. Sirtuins are histone deacetylases, which have 7 different subtypes (SIRT1-SIRT7) in mammals, regulate a variety of cellular functions, and play an important role in cell stress resistance, energy metabolism, apoptosis and aging. The regulation of metabolic balance by Sirtuins will directly affect various diseases related to metabolism. For example, SIRT1 regulates the acetylation state of histones with the participation of coenzyme I(NAD), and plays an important role in enhancing cardiac tolerance to oxidative stress, regulating myocardial energy metabolism and anti-aging.