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In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN).
The electron transport chain oxidizes coenzymes NADH and FADH2. Protein synthesis makes use of mitochondrial DNA, RNA, and tRNA. [5] Regulation of processes makes use of ions (Ca 2+ /K + /Mg +). [6] Additional metabolites present in the matrix are CO 2, H 2 O, O 2, ATP, ADP, and P i. [1]
General chemical structure of an acyl-CoA, where R is a carboxylic acid side chain. Acyl-CoA is a group of CoA-based coenzymes that metabolize carboxylic acids. Fatty acyl-CoA's are susceptible to beta oxidation, forming, ultimately, acetyl-CoA. The acetyl-CoA enters the citric acid cycle, eventually forming several equivalents of ATP. In this ...
This reaction is essential for the subsequent steps in beta oxidation that lead to the production of acetyl-CoA, NADH, and FADH2, which are important for generating ATP, the energy currency of the cell. Long-chain hydroxyacyl-CoA dehydrogenase (LCHAD) deficiency is a condition that affects mitochondrial function due to enzyme impairments.
Long-chain acyl-CoA esters are substrates for a number of important enzymatic reactions and play a central role in the regulation of metabolism as allosteric regulators of several enzymes. To participate in specific metabolic processes, fatty acids must first be activated by being joined in thioester linkage (R-CO-SCoA) to the -SH group of ...
An electron transport chain (ETC [1]) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H + ions) across a membrane.
The medium chain acyl-CoA dehydrogenase (MCAD) is the best known structure of all ACADs, and is the most commonly deficient enzyme within the class that leads to metabolic disorders in animals. [1] This protein is a homotetramer with each subunit containing roughly 400 amino acids and one equivalent of FAD per monomer.
The B chain of dipicolinate synthase, an enzyme which catalyses the formation of dipicolinic acid from dihydroxydipicolinic acid [13] Phenylacrylic acid decarboxylase (EC 4.1.1.102), an enzyme which confers resistance to cinnamic acid in yeast [14] Phototropin and cryptochrome, light-sensing proteins [15]