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同工酶变体的结构灵活性:果蝇中被辅因子和亚基结合掩盖的遗传变体。

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

作者信息

Johnson G B

出版信息

Proc Natl Acad Sci U S A. 1978 Jan;75(1):395-9. doi: 10.1073/pnas.75.1.395.

DOI:10.1073/pnas.75.1.395
PMID:203939
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC411255/
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.

摘要

野生的莫哈韦果蝇种群中,无NAD⁺形式的乙醇脱氢酶(乙醇:NAD⁺氧化还原酶;EC 1.1.1.1)呈现出相当大的构象变异。这种变异似乎是遗传性的,因为在近交系中不会出现。同一果蝇个体中存在的与NAD⁺结合的乙醇脱氢酶形式并未表现出这种变异,这表明NAD⁺的结合起到稳定构象的作用。因此,这种辅因子与酶的结合可能掩盖了相当大的变异。酯酶亚基的结合也有类似的作用。

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