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Flavin adenine dinucleotide consists of two portions: the adenine nucleotide (adenosine monophosphate) and the flavin mononucleotide (FMN) bridged together through their phosphate groups. Adenine is bound to a cyclic ribose at the 1' carbon, while phosphate is bound to the ribose at the 5' carbon to form the adenine nucledotide.
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.
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'). NADPH is the reduced form, whereas NADP + is the ...
Their action results in the introduction of a trans double-bond between C2 (α) and C3 (β) of the acyl-CoA thioester substrate. [1] Flavin adenine dinucleotide (FAD) is a required co-factor in addition to the presence of an active site glutamate in order for the enzyme to function.
The flavin is generally tightly bound (as in adrenodoxin reductase, wherein the FAD is buried deeply). [1] About 5-10% of flavoproteins have a covalently linked FAD. [ 2 ] Based on the available structural data, FAD-binding sites can be divided into more than 200 different types.
This means that it is a bisubstrate-biproduct mechanism. First the flavin reductase enzyme binds NADPH and stabilizes the release of the hydride. Because of sterics, it is not possible for the enzyme to bind both NADPH and the flavin. [5] For this reason, NADP+ is released and then the flavin substrate is bound to the enzyme.
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.
Thus, the two substrates of this enzyme are [[acyl-[acyl-carrier-protein]]] and NADP +, whereas its 3 products are [[trans-2,3-dehydroacyl-[acyl-carrier-protein]]], NADPH, and H +. This enzyme belongs to the family of oxidoreductases , to be specific, those acting on the CH-CH group of donor with NAD+ or NADP+ as acceptor.