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. 1978 Jan;75(1):395-9.
doi: 10.1073/pnas.75.1.395.

Structural flexibility of isozyme variants: genetic variants in Drosophila disguised by cofactor and subunit binding

G B Johnson

Structural flexibility of isozyme variants: genetic variants in Drosophila disguised by cofactor and subunit binding

G B Johnson. Proc Natl Acad Sci U S A. 1978 Jan.

Abstract

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.

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