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去抑制蛋白在ATP、镁依赖的蛋白磷酸酶相互转化中的作用

Role of the deinhibitor protein in the interconversion of the ATP,Mg-dependent protein phosphatase.

作者信息

Goris J, Waelkens E, Merlevede W

出版信息

Biochem Biophys Res Commun. 1983 Oct 14;116(1):349-54. doi: 10.1016/0006-291x(83)90421-7.

Abstract

The small molecular weight (+/- 9,000) heat stable deinhibitor protein, isolated from dog liver, not only protects the multisubstrate protein phosphatase from inhibition by inhibitor-1 and the modulator protein. It prevents the conversion of the active enzyme to the ATP,Mg-dependent enzyme form brought about by the modulator protein, and also affects the activation of the ATP,Mg-dependent protein phosphatase, probably by stabilizing the enzyme in its active conformation during the reversible activation by protein kinase FA. Therefore the deinhibitor protein could be an important factor in the process of glycogen synthesis, which requires glycogen synthase and phosphorylase as dephosphorylated enzymes.

摘要

从小狗肝脏中分离得到的小分子质量(约9000)热稳定去抑制蛋白,不仅能保护多底物蛋白磷酸酶不被抑制因子-1和调节蛋白所抑制。它能阻止调节蛋白导致的活性酶向ATP、Mg依赖酶形式的转变,还可能通过在蛋白激酶FA可逆激活过程中稳定酶的活性构象,影响ATP、Mg依赖蛋白磷酸酶的激活。因此,去抑制蛋白可能是糖原合成过程中的一个重要因素,糖原合成需要糖原合酶和磷酸化酶作为去磷酸化酶。

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