环磷酸腺苷和果糖-2,6-二磷酸刺激酵母果糖-1,6-二磷酸酶的体外磷酸化。
Cyclic AMP and fructose-2,6-bisphosphate stimulated in vitro phosphorylation of yeast fructose-1,6-bisphosphatase.
作者信息
Pohlig G, Wingender-Drissen R, Noda T, Holzer H
出版信息
Biochem Biophys Res Commun. 1983 Aug 30;115(1):317-24. doi: 10.1016/0006-291x(83)91006-9.
Phosphorylation of purified yeast fructose-1,6-bisphosphatase was studied using purified preparations from yeast of two different cyclic AMP-independent protein kinases and a cyclic AMP-dependent protein kinase. Incorporation of 32P into fructose-1,6-bisphosphatase could be demonstrated only with the cyclic AMP-dependent protein kinase. Phosphorylation of fructose-1,6-bisphosphatase was stimulated by 3 microM fructose-2,6-bisphosphate and inhibited by 1 mM 5'-AMP.
利用从酵母中纯化得到的两种不同的非环磷酸腺苷依赖性蛋白激酶和一种环磷酸腺苷依赖性蛋白激酶的制剂，对纯化的酵母果糖-1,6-二磷酸酶的磷酸化进行了研究。只有环磷酸腺苷依赖性蛋白激酶才能使果糖-1,6-二磷酸酶掺入32P。3 microM果糖-2,6-二磷酸刺激果糖-1,6-二磷酸酶的磷酸化，而1 mM 5'-AMP则抑制其磷酸化。
Zotero 插件