https://wiki.tiffa.net/w/index.php?action=history&feed=atom&title=Translations%3AFlavin_adenine_dinucleotide%2F54%2FenTranslations:Flavin adenine dinucleotide/54/en - Revision history2026-05-14T14:28:02ZRevision history for this page on the wikiMediaWiki 1.43.0https://wiki.tiffa.net/w/index.php?title=Translations:Flavin_adenine_dinucleotide/54/en&diff=136833&oldid=prevFuzzyBot: Importing a new version from external source2024-04-10T10:54:11Z<p>Importing a new version from external source</p>
<p><b>New page</b></p><div>New [[drug design|design]] of anti-bacterial medications is of continuing importance in scientific research as bacterial antibiotic resistance to common antibiotics increases. A specific metabolic protein that uses FAD ([[succinate dehydrogenase|Complex II]]) is vital for bacterial virulence, and so targeting FAD synthesis or creating FAD analogs could be a useful area of investigation. Already, scientists have determined the two structures FAD usually assumes once bound: either an extended or a butterfly conformation, in which the molecule essentially folds in half, resulting in the stacking of the adenine and isoalloxazine rings. FAD imitators that are able to bind in a similar manner but do not permit protein function could be useful mechanisms of inhibiting bacterial infection. Alternatively, drugs blocking FAD synthesis could achieve the same goal; this is especially intriguing because human and bacterial FAD synthesis relies on very different enzymes, meaning that a drug made to target bacterial FAD synthase would be unlikely to interfere with the human FAD synthase enzymes.</div>FuzzyBot