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NAD is a coenzyme formed from the nucleotide, nicotinamide, adenosine monophosphate, and a phosphate group joining the first two components. NADP has the same structure with the addition of an extra phosphate group to AMP. NAD can be reduced to NADH during coupling with reactions which oxidize various organic substrates. For example, the reaction catalyzed by glyceraldehyde phosphate dehydrogenase during glycolysis. NADH then passes to the inside of mitochondria where it donates the electrons it is carrying to the electron transport chain. In this manner, NAD acts as an intermediate energy storage compound that indirectly generates ATP. Generally, NADP accepts electrons from catabolic reactions to form NADPH. An example is its coupling with the conversion of glucose-6-phosphate to ribose-5-phosphate in the pentose phosphate pathway. NADPH has a slightly different role to NADH in that it does not donate electrons to the electron transport chain. Instead, it tends to reduce intermediates in anabolic pathways e.g. fatty acid synthesis. NAD participates in many redox reactions in cells, including those in glycolysis and most of those in the citric acid cycle of cellular respiration. Nicotinamide adenine dinucleotide (NAD) and its relative nicotinamide adenine dinucleotide phosphate (NADP) are two of the most important coenzymes in the cell. In cells, most oxidations are accomplished by the removal of hydrogen atoms. Both of these coenzymes play crucial roles in this. Each molecule of NAD+ (or NADP+) can acquire two electrons, that is, be reduced by two electrons. However, only one proton accompanies the reduction. The other proton produced as two hydrogen atoms are removed from the molecule being oxidized is liberated into the surrounding medium. For NAD, the reaction is thus , NAD+ + 2H -> NADH + H+, Appearance: Supplied as a white to pale yellow crystalline powder, Purity: >97%, Moisture: <10%, Absorbance Ratio: A250/A260: 0.83 ± 0.03, A280/A260: 0.22 ± 0.02, Country of Origin: Japan
This website uses cookies, which are necessary for the technical operation of the website and are always set. Other cookies, which increase the usability of this website, serve for direct advertising or simplify interaction with other websites and social networks, will only be used with your consent.
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