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The 3 substrates of this enzyme are FMNH2, NAD +, and NADP +, whereas its 4 products are FMN, NADH, NADPH, and H +. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is FMNH2:NAD(P)+ oxidoreductase.
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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 +
Elongation to stearate (18:0) mainly occurs in the ER by several membrane-bound enzymes. The steps involved in the elongation process are principally the same as those carried out by FAS, but the four principal successive steps of the elongation are performed by individual proteins, which may be physically associated. [5] [6]
The high reduction potential of the N2 cluster and the relative proximity of the other clusters in the chain enable efficient electron transfer over long distance in the protein (with transfer rates from NADH to N2 iron-sulfur cluster of about 100 μs). [12] [13] The equilibrium dynamics of Complex I are primarily driven by the quinone redox cycle.
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NADH + NADP + + H + outside => NAD + + NADPH + H + inside. This redox reaction is a transfer of hydride equivalents from NADH to NADP + coupled to a translocation of protons across a membrane. NADP + is reduced to NADPH by NADH, which is oxidized into NAD +. This reduction is tied to the inward translocation of protons across a membrane. [2]
Mechanism 1. Hydride transfer occurs by addition of H + and 2 e −: Mechanism 2. Hydride transfer by abstraction of hydride from NADH: Mechanism 3. Radical formation by electron abstraction: Mechanism 4. The loss of hydride to electron deficient R group: Mechanism 5. Use of nucleophilic addition to break R 1-R 2 bond: Mechanism 6.