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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.
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 +
Flavin mononucleotide (FMN), or riboflavin-5′-phosphate, is a biomolecule produced from riboflavin (vitamin B 2) by the enzyme riboflavin kinase and functions as the prosthetic group of various oxidoreductases, including NADH dehydrogenase, as well as a cofactor in biological blue-light photo receptors. [1]
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[10] While under standard conditions malate cannot reduce the more electronegative NAD +:NADH couple, in the cell the concentration of oxaloacetate is kept low enough that Malate dehydrogenase can reduce NAD + to NADH during the citric acid cycle. Fumarate + 2 H + + 2 e − → Succinate +0.03 [9] O 2 + 2H + + 2e − → H 2 O 2 +0.30
The pyruvate produced by glycolysis is an important intermediary in the conversion of carbohydrates into fatty acids and cholesterol. [7] This occurs via the conversion of pyruvate into acetyl-CoA in the mitochondrion. However, this acetyl-CoA needs to be transported into cytosol where the synthesis of fatty acids and cholesterol occurs.
Glutamate synthase catalyzes the conversion of 2-oxoglutarate into L-glutamate with L-glutamine serving as the nitrogen source for the reaction. All glutamate syntheses are iron-sulfur flavoproteins containing an iron-sulfur cluster and FMN. The three classes of glutamate syntheses are categorized based on their sequences and biochemical ...
This image of a simple structural formula is ineligible for copyright and therefore in the public domain, because it consists entirely of information that is common property and contains no original authorship.