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In enzymology, an FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction FMNH 2 + NAD(P)+ ⇌ {\displaystyle \rightleftharpoons } FMN + NAD(P)H + H + The 3 substrates of this enzyme are FMNH2 , NAD + , and NADP + , whereas its 4 products are FMN , NADH , NADPH , and H + .
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FMN reductase (NADH) (EC 1.5.1.42, NADH-FMN reductase) is an enzyme with systematic name FMNH 2: ... This enzyme catalyses the following chemical reaction. FMNH 2 ...
FMN reductase (NAD(P)H) (EC 1.5.1.39, FRG) is an enzyme with systematic name FMNH 2:NAD(P) + oxidoreductase. [1] This enzyme catalyses the following chemical reaction FMNH2 + NAD(P) + ⇌ {\displaystyle \rightleftharpoons } FMN + NAD(P)H + H +
NADP(H) and NAD(H) are equal and opposite contributors to metabolism, and this enzyme is necessary to keep a balance between the two. It can also function to generate a proton gradient across a membrane, as it is a reversible reaction, and is used as such in certain organisms.
In enzymology, a dihydropyrimidine dehydrogenase (NADP+) (EC 1.3.1.2) is an enzyme that catalyzes the chemical reaction. 5,6-dihydrouracil + NADP + uracil + NADPH + H + Thus, the two substrates of this enzyme are 5,6-dihydrouracil and NADP +, whereas its 3 products are uracil, NADPH, and H +.
The name "dehydrogenase" is based on the idea that it facilitates the removal (de-) of hydrogen (-hydrogen-) and is an enzyme (-ase). Dehydrogenase reactions come most commonly in two forms: the transfer of a hydride and release of a proton (often with water as a second reactant), and the transfer of two hydrogens.
The NADP + structural site is located greater than 20Å away from the substrate binding site and the catalytic coenzyme NADP + binding site. Its purpose in the enzyme catalyzed reaction has been unclear for many years. For some time, it was thought that NADP + binding to