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In oxidation-reduction reactions, the active part of the cofactor is the nicotinamide. In NAD + , the nitrogen in the aromatic nicotinamide ring is covalently bonded to adenine dinucleotide. The formal charge on the nitrogen is stabilized by the shared electrons of the other carbon atoms in the aromatic ring.
Nicotinamide adenine dinucleotide consists of two nucleosides joined by pyrophosphate. The nucleosides each contain a ribose ring, one with adenine attached to the first carbon atom (the 1' position) (adenosine diphosphate ribose) and the other with nicotinamide at this position. [4] [5] The redox reactions of nicotinamide adenine dinucleotide
Nicotinamide cofactor analogues have been synthesized with varying substituents on the dihydropyridine ring to tune their redox potential and stability, to replace NADH or NADPH in certain enzymatic reactions.
Nicotinamide adenine dinucleotide phosphate, abbreviated NADP [1] [2] or, in older notation, TPN (triphosphopyridine nucleotide), 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 ('hydrogen source').
NAD + kinase (EC 2.7.1.23, NADK) is an enzyme that converts nicotinamide adenine dinucleotide (NAD +) into NADP + through phosphorylating the NAD + coenzyme. [6] NADP + is an essential coenzyme that is reduced to NADPH primarily by the pentose phosphate pathway to provide reducing power in biosynthetic processes such as fatty acid biosynthesis and nucleotide synthesis. [7]
NMNH (Dihydronicotinamide mononucleotide), also known as reduced nicotinamide mononucleotide. [1] Both NMNH and NMN increase NAD+ levels in the body. [1] NAD+ is a universal coenzyme that plays vital roles in nearly all living organisms functioning in various biological processes such as metabolism, cell signaling, gene regulation, and DNA repair.
NADPH oxidase (nicotinamide adenine dinucleotide phosphate oxidase) is a membrane-bound enzyme complex that faces the extracellular space. It can be found in the plasma membrane as well as in the membranes of phagosomes used by neutrophil white blood cells to engulf microorganisms.
In redox biocatalysis, the nicotinamide cofactor (NAD(P)H or NAD(P)+) can act as an electron donor or acceptor by releasing or accepting a hydride. The cofactor must be used in the reaction either in stoichiometric amounts leading to inhibition and economic issues, or in catalytic amounts coupled with an in situ regeneration system.