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

100%

Frajnt M., Cytrynska M., Jakubowicz T.

Acta Biochimica Polonica

2003

tom 50

nr 4

Cyclic AMP dependent protein kinase (PKA) from Pichia pastoris yeast cells was found to be activated by either cAMP or cGMP. Analogs of cAMP such as 8-chloro-cAMP and 8-bromo-cAMP were as potent as cAMP in PKA activation while N6, 2'- O-dibutyryl-cAMP did not stimulate the enzyme activity. It was shown that protamine sulfate was almost equally phosphorylated in the presence of 1-2 X 10-6 M cAMP or cGMP while other substrates such as Kemptide, ribosomal protein S6 were phosphorylated to a lower extent in the presence of cGMP. It was demonstrated that pyruvate kinase is a substrate of PKA which co-purified with the P. pastoris enzyme. Moreover, pyruvate kinase was phosphorylated by PKA in the presence of cAMP and cGMP to comparable levels.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Cytrynska M.

1 Frajnt M.

1 Jakubowicz T.

1 2003

Wyniki wyszukiwania

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