Protein Kinase A from bovine heart has been used to determine its activity using a molecular beacon probe. It has also been used to study the interaction of staurosporine with the ATP-binding site of kinases.
Protein Kinase A (PKA) is a serine/threonine kinase, which exists as a tetrameric holoenzyme.
Protein Kinase A (PKA) inhibits hormone-sensitive lipase translocation from cytosol to storage droplets and blocks lipolysis. It regulates apoptosis, mitochondrial respiration and ATP synthesis. PKA is modulated by protease calpain.
