scholarly journals Dephosphorylation of Catalytic Subunit of cAMP-dependent Protein Kinase at Thr-197 by a Cellular Protein Phosphatase and by Purified Protein Phosphatase-2A

1996 ◽  
Vol 271 (1) ◽  
pp. 258-263 ◽  
Author(s):  
Susanne Liauw ◽  
Robert A. Steinberg
Keyword(s):  
Protein Kinase ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Cellular Protein ◽  
Catalytic Subunit ◽  
Dependent Protein Kinase ◽  
Camp Dependent Protein Kinase ◽  
Phosphatase 2A ◽  
Dependent Protein

scholarly journals Fructose-2,6-bisphosphatase and 6-phosphofructo-2-kinase are separable in yeast

1987 ◽  
Vol 246 (3) ◽  
pp. 755-759 ◽  
Author(s):  
M Kretschmer ◽  
W Schellenberger ◽  
A Otto ◽  
R Kessler ◽  
E Hofmann
Keyword(s):  
Alkaline Phosphatase ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Phosphatase ◽  
Protein Phosphatase 2A ◽  
Dependent Protein Kinase ◽  
Km Value ◽  
Phosphatase 2A ◽  
Dependent Protein

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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