Nicotinamide Adenine Dinucleotide Phosphate

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Nicotinamide adenine dinucleotide phosphate (NADP)

A coenzyme and an important component of the enzymatic systems concerned with biological oxidation-reduction systems. It is also known as NAD, triphosphopyridine nucleotide (TPN), coenzyme II, and codehydrogenase II. The compound is similar in structure and function to nicotinamide adenine dinucleotide (NAD). It differs structurally from NAD in having an additional phosphoric acid group esterified at the 2 position of the ribose moiety of the adenylic acid portion. In biological oxidation-reduction reactions the NADP molecule becomes alternately reduced to its hydrogenated form (NADPH) and reoxidized to its initial state (see illustration). See Carbohydrate metabolism, Coenzyme, Enzyme

Triphosphopyridine nucleotideenlarge picture
Triphosphopyridine nucleotide

Nicotinamide Adenine Dinucleotide Phosphate


(NADP; also called triphosphopyridine nucleotide, or TPN; obsolete term, coenzyme II and codehydrogenase II), a common coenzyme. Like nicotinamide adenine dinucleotide, NADP is found in all types of cells, where it participates in oxidation-reduction reactions. Its structure was established in 1934 by O. Warburg. It serves as a hydrogen acceptor during the oxidation mainly of carbohydrates; in its reduced form it is a hydrogen donor during the biosynthesis of fatty acids. In the chloroplasts of plant cells, NADP is reduced during the light reactions of photosynthesis and then provides hydrogen for the synthesis of carbohydrates during dark reactions.

nicotinamide adenine dinucleotide phosphate

[‚nik·ə¦tin·e‚mīd ′ad·ən‚ēn dī¦nü·klē·ə‚tīd ′fäs‚fāt]
(cell and molecular biology)
A coenzyme and important component of the enzymatic systems concerned with biological oxidation-reduction systems. Abbreviated NADP+ (the reduced form is abbreviated NADPH).
References in periodicals archive ?
We have recently used just such a method, coupled with a Laue x-ray diffraction experiment, to define the structure of the Miehaelis complex of the enzyme isocitrate dehydrogenase (IDH), its substrate isocitrate, cofactor nicotinamide adenine dinucleotide phosphate (NADP+) and magnesium [2].
Chronic granulomatous disease (CGD) is a relatively rare genetic disorder characterised by defect in respiratory burst activity of phagocytes that is associated with intracellular killing of phagocytosed microorganisms.1 In CGD, the primary defect is associated with the key enzyme, nicotinamide adenine dinucleotide phosphate (NADPH) oxidase.
One of the main sources of [O.sub.2.sup.*-] in living organisms is nicotinamide adenine dinucleotide phosphate oxidase (NADPH oxidase); however, uncoupled nitric oxide synthase (NOS) may also be a significant source of ROS [9].
The definitive treatment of methemoglobinemia is the use of the reducing agent, methylene blue whose action is dependent on production of the reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) by the hexose phosphate shunt and the activity of the enzyme, NADPH-methemoglobin reductase.
However, TCB exhibited estrogenic activity after incubation with liver microsomes of phenobarbital-treated rats in the presence of reduced nicotinamide adenine dinucleotide phosphate (NADPH).
It is now known that hyperglycaemic conditions of cells are associated with the enhanced levels of ROS mainly generated by mitochondria and nicotinamide adenine dinucleotide phosphate (NADPH) oxidase.

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