Open AccessStructural flexibility of isozyme variants: genetic variants in Drosophila disguised by cofactor and subunit binding.
Author(s) -
George B. Johnson
Publication year - 1978
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.1.395
Subject(s) - nad+ kinase , isozyme , cofactor , alcohol dehydrogenase , oxidoreductase , protein subunit , biology , biochemistry , alcohol oxidoreductase , genetics , enzyme , drosophila melanogaster , esterase , gene
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.