scholarly journals Protein Phosphatase 2A Is Associated with Class C L-type Calcium Channels (Cav1.2) and Antagonizes Channel Phosphorylation by cAMP-dependent Protein Kinase

2000 ◽  
Vol 275 (50) ◽  
pp. 39710-39717 ◽  
Author(s):  
Monika A. Davare ◽  
Mary C. Horne ◽  
Johannes W. Hell
1987 ◽  
Vol 246 (3) ◽  
pp. 755-759 ◽  
Author(s):  
M Kretschmer ◽  
W Schellenberger ◽  
A Otto ◽  
R Kessler ◽  
E Hofmann

Fructose-2,6-bisphosphatase was purified from yeast and separated from 6-phosphofructo-2-kinase and alkaline phosphatase. The enzyme released Pi from the 2-position of fructose 2,6-bisphosphate and formed fructose 6-phosphate in stoichiometric amounts. The enzyme displays hyperbolic kinetics towards fructose 2,6-bisphosphate, with a Km value of 0.3 microM. It is strongly inhibited by fructose 6-phosphate. The inhibition is counteracted by L-glycerol 3-phosphate. Phosphorylation of the enzyme by cyclic-AMP-dependent protein kinase causes inactivation, which is reversible by the action of protein phosphatase 2A.


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