cAMP-dependent protein kinase


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cAMP-dependent protein kinase

a tetrameric protein composed of two regulatory subunits that bind cAMP, and two catalytic subunits that catalyze the transfer of a phosphoryl group from ATP to a target enzyme.
References in periodicals archive ?
Regulation of cAMP-dependent Protein Kinase during appressorium formation in Magnaporthe grisea.
and first found cAMP-dependent protein kinase in brain in the world.
alpha] of mouse cAMP-dependent protein kinase (protein kinase A), recombinantly expressed in E.
Stereochemical course of the phospho group transfer catalyzed by cAMP-dependent protein kinase.
The enzyme was stoichio-metrically phosphorylated in the presence of the catalytic subunit of the cAMP-dependent protein kinase (Biaffin GmbH & Ko, Kessel, Germany) and ATP.
Comparison of cAMP-dependent protein kinase substrate specificity in reaction with proteins and synthetic peptides.
Holoenzymes of cAMP-dependent protein kinase containing the neural form of type I regulatory subunit have an increased sensitivity to cyclic nucleotides.
Synergistic binding of nucleotides and inhibitors to cAMP-dependent protein kinase examined by acrylodan fluorescence spectroscopy.
cAMP-dependent protein kinase (PKA) is a multi functional enzyme regulating processes such as signaling, gene expression, anti cellular proliferation.
1990), this assay is based upon the specific phosphorylation by PKC of an 11-amino acid peptide sequence of myelin basic protein, which is not phosphorylated by either cAMP-dependent protein kinase (PKA), casein kinases I and II, [Ca.
Coordinated control of endothelial nitric-oxide synthase phosphorylation by protein kinase C and the cAMP-dependent protein kinase.

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