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NADPH is the reduced form, whereas NADP + is the oxidized form. NADP + is used by all forms of cellular life. NADP + is essential for life because it is needed for cellular respiration. [3] NADP + differs from NAD + by the presence of an additional phosphate group on the 2' position of the ribose ring that carries the adenine moiety.
NADP is a reducing agent in anabolic reactions like the Calvin cycle and lipid and nucleic acid syntheses. NADP exists in two forms: NADP+, the oxidized form, and NADPH, the reduced form. NADP is similar to nicotinamide adenine dinucleotide (NAD), but NADP has a phosphate group at the C-2′ position of the adenosyl.
In E. coli, this pathway contribute equal amounts of NADPH as the pentose phosphate pathway, and both were the main producers of NADPH under standard growth conditions. [4] NADP(H) and NAD(H) are equal and opposite contributors to metabolism, and this enzyme is necessary to keep a balance between the two.
One of the uses of NADPH in the cell is to prevent oxidative stress. It reduces glutathione via glutathione reductase, which converts reactive H 2 O 2 into H 2 O by glutathione peroxidase. If absent, the H 2 O 2 would be converted to hydroxyl free radicals by Fenton chemistry, which can attack the cell. Erythrocytes, for example, generate a ...
The reasoning behind having two separate electron carriers for anabolic and catabolic pathways relates to regulation of metabolism. [7] The ratio of NADP + to NADPH in the cell is kept rather low, so that NADPH is readily available as a reducing agent; it is more commonly used as a reducing agent than NADP + is used as an oxidizing agent. [8]
The source of the NADPH is two-fold. When malate is oxidatively decarboxylated by "NADP +-linked malic enzyme" to form pyruvate, CO 2 and NADPH are formed. NADPH is also formed by the pentose phosphate pathway which converts glucose into ribose, which can be used in synthesis of nucleotides and nucleic acids, or it can be catabolized to ...
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.
p-Hydroxybenzoate hydroxylase (PHBH) catalyzes the oxygenation of p-hydroxybenzoate (pOHB) to 3,4-dihyroxybenzoate (3,4-diOHB); FAD, NADPH and molecular oxygen are all required for this reaction. NADPH first transfers a hydride equivalent to FAD, creating FADH −, and then NADP + dissociates from the enzyme. Reduced PHBH then reacts with ...