Autophosphorylation of cGMP‐dependent protein kinase is stimulated only by occupancy of one the two cGMP binding sites

FEBS Letters

Hofmann, Franz¹  Gensheimer, Hans-Peter¹  Gobel, Claus¹ 

[1] Pharmakologisches Institut der Unversität, Im Neuenheirmer Feld 366, 6900 Heidelberg, FRG

关键词: Autophosphorylation;    cGMP-dependent protein kinase;    8-Benzyl-amino-cAMP;    N 2-Monobutyryl-c-GMP;   

DOI  :  10.1016/0014-5793(83)80315-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

cGMP-Dependent protein kinase contains, per subunit, 2 binding for cGMP. The apparent K _D values for site 1 and 2 were 12 and 55 nM. The analogues 8-benzyl-amino-cAMP and N ²-monobutyryl-cGMP bind preferentially to site 1 and 2, respectively. Both analogues stimulate autophosphorylation of the enzyme at concentrations at which only half of the phosphotrasferase activity of the enzyme is expressed. Complete expression of the phosphotransferase activity requires a high concentration of each analogue and is accompanied by inhibition of the autophosphorylation reactions. It is concluded that occupancy of site 1 or 2 stimulates autophosphorylation while occupancy of both sites prevents autophosphorylation.

【 授权许可】

Unknown