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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').
A biological coenzyme that acts as an electron carrier in enzymatic reactions. 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.
Rather, NADP-ME was directly transformed from a C 3 species in photosynthesis, and even earlier origins from an ancient cystolic ancestor. In the cytosol, the enzyme existed as a series of housekeeping isoforms purposed towards a variety of functions including malate level maintenance during hypoxia, microspore separation, and pathogen defense.
In enzymology, a malate dehydrogenase (NADP +) (EC 1.1.1.82) is an enzyme that catalyzes the chemical reaction (S)-malate + NADP + oxaloacetate + NADPH + H +. Thus, the two substrates of this enzyme are (S)-malate and NADP +, whereas its 3 products are oxaloacetate, NADPH, and H +.
In the plant-like family of FNRs, selective evolutionary pressure has led to differences in the catalytic efficiency of FNRs in photosynthetic and nonphotosynthetic organisms. Electron transfer by FNR is a rate limiting step in photosynthesis, so the plastidic FNR in plants have evolved to be highly efficient. [8]
Oxidoreductases, enzymes that catalyze oxidation-reduction reactions, constitute Class EC 1 of the IUBMB classification of enzyme-catalyzed reactions. [2] Any of these may be called dehydrogenases, especially those in which NAD + is the electron acceptor (oxidant), but reductase is also used when the physiological emphasis on reduction of the substrate, and oxidase is used only when O 2 is the ...
Four different subunits were found to be important for the function of the photosynthetic reaction center. The L and M subunits, shown in blue and purple in the image of the structure, both span the lipid bilayer of the plasma membrane. They are structurally similar to one another, both having 5 transmembrane alpha helices. [6]
The structure and function of cytochrome b 6 f (in chloroplasts) is very similar to cytochrome bc 1 (Complex III in mitochondria). Both are transmembrane structures that remove electrons from a mobile, lipid-soluble electron carrier (plastoquinone in chloroplasts; ubiquinone in mitochondria) and transfer them to a mobile, water-soluble electron ...