nicotinamide adenine dinucleotide phosphate


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nic·o·tin·a·mide ad·e·nine di·nu·cle·o·tide phos·phate (NADP, NADP+, NADPH),

(nik'ō-tin'ă-mīd ad'ĕ-nīn dī-nū'klē-ō-tīd fos'fāt),
A coenzyme of many oxidases (dehydrogenases), in which the reaction NADP+ + 2H ⇋ NADPH + H+ takes place; the third phosphoric group esterifies the 2'-hydroxyl of the adenosine moiety of NAD+.

nic·o·tin·a·mide ad·e·nine di·nu·cle·o·tide phos·phate

(NADP) (nik'ō-tin'ă-mīd ad'ĕ-nēn dī-nū'klē-ō-tīd fos'fāt)
A coenzyme of many oxidases (dehydrogenases), in which the reaction NADP+ + 2H → NADPH + H+ takes place; the third phosphoric group esterifies the 2'-hydroxyl of the adenosine moiety of NAD.

nicotinamide adenine dinucleotide phosphate

Abbreviation: NADP
A coenzyme that contains adenosine, nicotinamide, and phosphoric acid. When in its oxidized form (NADP+), it serves as an electron carrier in catabolic and anabolic reactions. In its reduced form (NADPH or NADPH-diaphorase), it is important in reducing the ferric iron (Fe+++) to its ferrous (Fe++) form, thus converting methemoglobin (which is unable to transport oxygen) to hemoglobin (which can transport oxygen). Deficiency of NADPH-diaphorase causes congenital methemoglobinemia.
Synonym: methemoglobin reductase
See also: nicotinamide
References in periodicals archive ?
Reduced glutathione (GSH), 1-chloro-2,4-dinitrobenzene (CDNB), reduced nicotinamide adenine dinucleotide phosphate (NADPH), amidopyrine, cytochrome C, thiobarbituric acid and all other chemicals were purchased from Sigma Chemical Company (Saint Louis, USA).
Utilization of oxygen and reduces nicotinamide adenine dinucleotide phosphate by human placental microsomes during aromatization of androstenedione.
The measurement is based on the fact that the enzymatic reduction of diacetyl requires the cofactor nicotinamide adenine dinucleotide phosphate (NADPH).
Superoxide anion production secondary to the assembly of the PMN nicotinamide adenine dinucleotide phosphate (reduced form; NADPH) oxidase is a standard measure of PMN activation.
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].

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