Hofmann K H, Polnisch E
Sektion Biologie, WB Technische Mikrobiologie, Ernst-Moritz-Arndt-Universität Greifswald.
J Basic Microbiol. 1990;30(8):555-9. doi: 10.1002/jobm.3620300805.
In crude extracts of Candida maltosa, about 12 proteins are phosphorylated in the presence of cAMP or of a catalytic subunit of cAMP-dependent protein kinase. A strongly labelled protein spot occurred in the position of fructose-1,6-bisphosphatase both after electrophoresis of crude extracts incubated with cAMP and of a partially purified fructose-1,6-bisphosphatase incubated with a catalytic subunit of cAMP-dependent protein kinase. No phosphorylation of the cytoplasmic malate dehydrogenase could be detected. From these results it was concluded that cAMP-dependent phosphorylation plays an important role in the catabolite inactivation of fructose-1,6-bisphosphatase in Candida maltosa, as described for Saccharomyces cerevisiae.
在麦芽糖假丝酵母的粗提物中，大约有12种蛋白质在存在环磷酸腺苷（cAMP）或cAMP依赖性蛋白激酶的催化亚基时会发生磷酸化。在用cAMP孵育的粗提物以及用cAMP依赖性蛋白激酶的催化亚基孵育的部分纯化的果糖-1,6-二磷酸酶进行电泳后，在果糖-1,6-二磷酸酶的位置出现了一个强标记的蛋白质斑点。未检测到细胞质苹果酸脱氢酶的磷酸化。从这些结果可以得出结论，如酿酒酵母中所描述的那样，cAMP依赖性磷酸化在麦芽糖假丝酵母中果糖-1,6-二磷酸酶的分解代谢失活中起重要作用。
