The effect of cAMP and cGMP on the activity and substrate specificity of protein kinase A from methylotrophic yeast Pichia pastoris.

作者: Magdalena Frajnt , Małgorzata Cytryńska , Teresa Jakubowicz

DOI: 10.18388/ABP.2003_3635

关键词: Phosphodiesterase 3Cell biologyPhosphorylationChemistryBiochemistryPyruvate kinaseEnzymeProtein kinase AProtein phosphorylationPDE10APichia 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

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