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葡萄糖激酶的调节蛋白与肝细胞膜结合,但与葡萄糖激酶不同的是,在底物刺激过程中它不会发生易位。

The regulatory protein of glucokinase binds to the hepatocyte matrix, but, unlike glucokinase, does not translocate during substrate stimulation.

作者信息

Agius L, Peak M, Van Schaftingen E

机构信息

Department of Medicine, University of Newcastle upon Tyne, U.K.

出版信息

Biochem J. 1995 Aug 1;309 ( Pt 3)(Pt 3):711-3. doi: 10.1042/bj3090711.

Abstract

The kinetic properties of hepatic glucokinase (hexokinase IV) are modulated by binding to a regulatory protein. This study shows that, in hepatocytes incubated with 5 mM glucose as sole carbohydrate substrate, both glucokinase and its regulatory protein bind to the cell matrix by a Mg(2+)-dependent mechanism. After incubation with an elevated [glucose] or with fructose, glucokinase, but not its regulatory protein, translocates from the Mg(2+)-dependent binding site. It is suggested that the regulatory protein acts as a receptor for anchoring glucokinase to the hepatocyte matrix and inhibiting its activity in metabolically quiescent conditions.

摘要

肝葡萄糖激酶(己糖激酶IV)的动力学特性通过与一种调节蛋白结合而受到调控。本研究表明,在以5 mM葡萄糖作为唯一碳水化合物底物孵育的肝细胞中,葡萄糖激酶及其调节蛋白均通过一种Mg(2+)依赖性机制与细胞基质结合。在用升高的[葡萄糖]或果糖孵育后,葡萄糖激酶会从Mg(2+)依赖性结合位点发生易位,但其调节蛋白不会。有人提出,调节蛋白作为一种受体,可将葡萄糖激酶锚定到肝细胞基质上,并在代谢静止状态下抑制其活性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ce63/1135689/93a3912117db/biochemj00058-0026-a.jpg

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