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	<title>Translations:Flavin adenine dinucleotide/15/en - Revision history</title>
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	<updated>2026-05-26T08:56:31Z</updated>
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		<title>FuzzyBot: Importing a new version from external source</title>
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		<updated>2024-04-10T10:54:10Z</updated>

		<summary type="html">&lt;p&gt;Importing a new version from external source&lt;/p&gt;
&lt;p&gt;&lt;b&gt;New page&lt;/b&gt;&lt;/p&gt;&lt;div&gt;FAD plays a major role as an enzyme [[Cofactor (biochemistry)|cofactor]] along with [[flavin mononucleotide]], another molecule originating from riboflavin. Bacteria, fungi and plants can produce [[riboflavin]], but other [[eukaryote]]s, such as humans, have lost the ability to make it. Therefore, humans must obtain riboflavin, also known as vitamin B2, from dietary sources. Riboflavin is generally ingested in the small intestine and then transported to cells via carrier proteins. [[Riboflavin kinase]] (EC 2.7.1.26) adds a phosphate group to riboflavin to produce flavin mononucleotide, and then [[FMN adenylyltransferase|FAD synthetase]] attaches an adenine [[nucleotide]]; both steps require [[adenosine triphosphate|ATP]]. Bacteria generally have one bi-functional enzyme, but [[archaea]] and eukaryotes usually employ two distinct enzymes. Current research indicates that distinct [[protein isoforms|isoforms]] exist in the [[cytosol]] and [[mitochondrion|mitochondria]]. It seems that FAD is synthesized in both locations and potentially transported where needed.&lt;br /&gt;
:[[Image:FAD Synthesis.png|250px]]&lt;/div&gt;</summary>
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