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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.

Content

Title variants

Languages of publication

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.

Keywords

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

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-abpv50i4p1111kz
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