Article
Enhanced dephosphorylation of cAMP-dependent protein kinase by oxidation and thiol modification.
The Journal of biological chemistry - 28 Jan 2005
Humphries Kenneth M, Deal Michael S, Taylor Susan S
Abstract excerpt
The catalytic subunit of cAMP-dependent protein kinase (PKA) is phosphorylated at threonine 197 and serine 338. Phosphorylation of threonine 197, located in the activation loop, is required for coordinating the active site conformation and optimal enzymatic activity. However, this phosphorylation has not been widely appreciated as a regulatory site because of the apparent constitutive nature of the...
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