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2003 | 50 | 4 | 1111-1118
Article title

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

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EN
Abstracts
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 × 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.
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Publisher

Year
Volume
50
Issue
4
Pages
1111-1118
Physical description
Dates
published
2003
received
2003-10-15
revised
2003-11-24
accepted
2003-12-08
Contributors
  • Department of Molecular Biology, Maria Curie-Skłodowska University, Lublin, Poland
  • Department of Invertebrate Immunology, Maria Curie-Skłodowska University, Lublin, Poland
  • Department of Invertebrate Immunology, Maria Curie-Skłodowska University, Lublin, Poland
References
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Document Type
Publication order reference
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YADDA identifier
bwmeta1.element.bwnjournal-article-abpv50i4p1111kz
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