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一种从鞘翅目昆虫(黄粉虫)脂肪体中纯化的海藻糖酶,被一种内源性胰岛素样肽进行分子激活。

Molecular activation of a trehalase purified from the fat body of a coleopteran insect (Tenebrio molitor), by an endogenous insulin-like peptide.

作者信息

Bounias M, Bahjou A, Gourdoux L, Moreau R

机构信息

Université d'Avignon, France.

出版信息

Biochem Mol Biol Int. 1993 Oct;31(2):249-66.

PMID:8275014
Abstract

Trehalase is the major factor involved in the release of glucose in the various insects organs. During physiological regulatory processes, and particularly during the induction or breaking of diapause, insulin-like factors are involved. Then, by contrast with the classical hypoglycemic role of insulin, the insulin-like peptide isolated from the insect (brain and/or fat body) is also able to activate the fat body trehalase in vitro, through a direct molecular interaction. The mechanism involves the binding of the activator to the "trehalase-trehalose complex", rather than on the free enzyme, without change in the Hill coefficient nor in the maximum velocity (Vmax). The rate constant KR is conversely proportional to the activator concentration. This mechanism can be totally quenched by adding an anti-serum anti-insulin-like factor in the reaction medium.

摘要

海藻糖酶是参与各种昆虫器官中葡萄糖释放的主要因素。在生理调节过程中,特别是在滞育诱导或解除期间,胰岛素样因子会参与其中。然而,与胰岛素经典的降血糖作用相反,从昆虫(脑和/或脂肪体)中分离出的胰岛素样肽在体外也能够通过直接的分子相互作用激活脂肪体海藻糖酶。其机制涉及激活剂与“海藻糖酶 - 海藻糖复合物”结合,而非与游离酶结合,且希尔系数和最大反应速度(Vmax)均无变化。相反,速率常数KR与激活剂浓度成反比。在反应介质中添加抗胰岛素样因子抗血清可完全抑制这一机制。

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