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Prebiotic origin of coenzymes. Like amino acids and nucleotides , certain vitamins and thus coenzymes can be created under early earth conditions. For instance, vitamin B3 can be synthesized with electric discharges applied to ethylene and ammonia . [ 69 ]
Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle.All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate.
Coenzymes Q is a coenzyme family that is ubiquitous in animals and many Pseudomonadota, [10] a group of gram-negative bacteria. The fact that the coenzyme is ubiquitous gives the origin of its other name, ubiquinone. [1] [2] [11] In humans, the most common form of coenzymes Q is coenzyme Q 10, also called CoQ 10 (/ ˌ k oʊ k j uː ˈ t ɛ n ...
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Since coenzymes are chemically changed as a consequence of enzyme action, it is useful to consider coenzymes to be a special class of substrates, or second substrates, which are common to many different enzymes. For example, about 1000 enzymes are known to use the coenzyme NADH. [62]
Coenzyme M is a coenzyme required for methyl-transfer reactions in the metabolism of archaeal methanogens, [1] [2] and in the metabolism of other substrates in bacteria. [3] It is also a necessary cofactor in the metabolic pathway of alkene-oxidizing bacteria.
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism.
The coenzyme Q : cytochrome c – oxidoreductase, sometimes called the cytochrome bc 1 complex, and at other times complex III, is the third complex in the electron transport chain (EC 1.10.2.2), playing a critical role in biochemical generation of ATP (oxidative phosphorylation).
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