Structural flexibility of isozyme variants: genetic variants in Drosophila disguised by cofactor and subunit binding.
Wild populations of Drosophila mojavensis exhibit considerable conformational variation in the NAD+-free form of alcohol dehydrogenase (alcohol:NAD+ oxidoreductase; EC 1.1.1.1). The variation appears genetic, as it does not occur within an inbred strain. The NAD+-bound form of alcohol dehydrogenase, present in the same individuals, does not exhibit the variation, suggesting that the binding of NAD+ acts to stabilize conformation. Such cofactor binding to enzymes may thus conceal considerable variation. A similar effect is suggested for binding of esterase subunits.
D000429:Alcohol Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D000818:Animals; D004330:Drosophila / Q000201:enzymology* / Q000235:genetics; D004950:Esterases / Q000032:analysis; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D009243:NAD / Q000378:metabolism; D011110:Polymorphism, Genetic; D011487:Protein Conformation
D007527:Isoenzymes; D009243:NAD; D000429:Alcohol Oxidoreductases; D004950:Esterases