cAMP-dependent protein kinase catalytic subunit beta (PRKACB) (PRKACB)

cAMP-dependent protein kinase catalytic subunit beta (PRKACB) is a critical enzyme in the cAMP-dependent signaling pathway, functioning as a serine/threonine kinase (UniProt P22694). It is part of the protein kinase A (PKA) holoenzyme, which remains inactive until cAMP binds to the regulatory subunits, releasing the catalytic subunits to phosphorylate target proteins like CREB (NCBI Gene ID: 5567). PRKACB plays a vital role in regulating glucose metabolism, cell cycle progression, and neuronal signaling (PubMed: 25635046). In disease contexts, mutations or over-expression of PRKACB are linked to endocrine disorders such as Cushing's syndrome and various malignancies (PubMed: 24572087). Pharmacological targeting of PRKACB typically involves ATP-competitive inhibitors, though the high structural homology between PKA isoforms presents a challenge for selectivity (PubChem CID: 3547). Current research focuses on identifying isoform-specific inhibitors to treat metabolic and oncogenic conditions while minimizing off-target effects (PubMed: 30135618).

Other names

Protein kinase A catalytic subunit betaPKA C-betaPRKACBPKACB

Catalyzes the transfer of the gamma-phosphoryl group from ATP to serine or threonine residues of substrate proteins in a cAMP-dependent manner (UniProt P22694).