N-myristylation of the catalytic subunit of cAMP-dependent protein kinase conveys structural stability

摘要: Coexpression of the yeast N-myristyltransferase with murine catalytic subunit cAMP-dependent protein kinase in prokaryotic cells results N-myristylation recombinant subunit. The acylated was purified following vitro holoenzyme formation a mutant form regulatory and compared to non-myristylated enzyme mammalian porcine enzyme. All three enzymes are very similar terms their kinetic properties capacity reassociate holoenzyme. In contrast, myristylated is significantly more stable thermal denaturation than Its stability now comparable subunits when they part complex. Each shows an increase T1/2 10 degrees C. This study demonstrates that one function for myristic acid at NH2 terminus provide structural stability.