Bovine brain adenosine 3',5'-monophosphate dependent protein kinase. Mechanism of regulatory subunit inhibition of the catalytic subunit.
作者： Jonathan J. Witt , Robert Roskoski
DOI: 10.1021/BI00691A026
关键词: Cyclin-dependent kinase complex 、 Casein kinase 2, alpha 1 、 Casein kinase 2 、 Biochemistry 、 Chemistry 、 Protein subunit 、 Protein kinase A 、 Gi alpha subunit 、 Gamma-aminobutyric acid receptor subunit alpha-1 、 Mitogen-activated protein kinase kinase
摘要: Adenosine 3',5'-monophosphate (cAMP) dependent protein kinase (EC 2.7.1.37) catalyzes the phosphorylation of serine and threonine residues a number proteins according to following chemical equation: ATP + leads phosphoprotein ADP. The DEAE-cellulose peak II holoenzyme from bovine brain, which is composed regulatory catalytic subunits, resistant ethoxyformic anhydride inactivation. After adding cAMP, becomes susceptible inhibition. Ethoxyformic (2mM) inhibits enzyme 50% (5 min, pH 6.5, 30 degrees) in presence 10 muM but less than 5% its absence. substrate, Mg2+-ATP, protects against inactivation suggesting that inhibition associated with modification active site. Addition subunit or Mg2+-ATP isolated also prevents These results suggest shields site thereby inhibiting it. In contrast brain muscle holoenzyme, I absence cAMP.
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