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

• Autorzy: Frajnt M. , Cytrynska M. , Jakubowicz T.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

yeast; cell; methylotrophic yeast; Pichia pastoris; protein phosphorylation; protein kinase; substrate specificity

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2003
• Tom: 50
• Numer: 4
• Opis fizyczny: p.1111-1118,fig.,ref.

Twórcy

autor

Frajnt M.

• Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland

autor

Cytrynska M.

autor

Jakubowicz T.

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