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Function
Protein Kinase A (PKA) helps animals cope with stressful situations. In the "flight or fight" response, muscle becomes primed for action as a result of the activity of PKA. Upon activation by cAMP, PKA alters the activities of target proteins by phopshorylating specific serine or threonine residues. This enzyme also helps regulate glucose levels. When activated by cAMP, PKA simultaneously catalyzes the breakdown of glycogen and inhibits the synthesis of glucose. (? makes sure this is right)
Structure
PKA consists of two types of subunits. It has a 49-kd regulatory subunit (R) and a 38-kd catalytic subunit (C).When PKA is enzymatically inactive (absence of cAMP), it is a tetrameric complex of a regulatory dimer bound to two catalytic subunits, forming the R2C2 complex. In its active state, the complex dissociates to form an R2 subunit and two C subunits. The catalytic subunit has two lobes. The larger lobe binds the peptide and contributes the key catalytic residues and the smaller lobe makes many contacts with ATP-Mg2+.
Mechanism
Regulation
Disease
Relevance
Structural highlights
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