- Tytuł:
- The effect of cAMP and cGMP on the activity and substrate specificity of protein kinase A from methylotrophic yeast Pichia pastoris.
- Autorzy:
-
Frajnt, Magdalena
Cytryńska, Małgorzata
Jakubowicz, Teresa - Powiązania:
- https://bibliotekanauki.pl/articles/1043395.pdf
- Data publikacji:
- 2003
- Wydawca:
- Polskie Towarzystwo Biochemiczne
- Tematy:
-
protein phosphorylation
cAMP
PKA
cGMP
yeast - Opis:
- 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 × 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.
- Źródło:
-
Acta Biochimica Polonica; 2003, 50, 4; 1111-1118
0001-527X - Pojawia się w:
- Acta Biochimica Polonica
- Dostawca treści:
- Biblioteka Nauki
Artykuł