作者: Magdalena Frajnt , Małgorzata Cytryńska , Teresa Jakubowicz
关键词: Phosphodiesterase 3 、 Cell biology 、 Phosphorylation 、 Chemistry 、 Biochemistry 、 Pyruvate kinase 、 Enzyme 、 Protein kinase A 、 Protein phosphorylation 、 PDE10A 、 Pichia pastoris
摘要: Cyclic AMP dependent protein kinase (PKA) from Pichia pastoris yeast cells was found to be activated by either cAMP or cGMP. Analogs of such as 8-chloro-cAMP and 8-bromo-cAMP were potent in PKA activation while N 6 ,2'-O-dibutyryl-cAMP did not stimulate the enzyme activity. It shown that protamine sulfate almost equally phosphorylated presence 1–2 10 –6 M cGMP other substrates Kemptide, ribosomal S 6, a lower extent demonstrated pyruvate is substrate which co-purified with P. enzyme. Moreover, comparable levels. plays key role regulation basic cellular pro