A Pseudo-Receptor Model of the Active Site of Protein Kinase C: An Example for a New Technique in Molecular Modelling

1995 ◽  
pp. 25-39
Author(s):  
C. W. v. d. Lieth ◽  
G. Krauter ◽  
E. Hecker
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Molecular Modelling ◽  
Active Site ◽  
New Technique ◽  
Receptor Model ◽  
Kinase C ◽  
A New Technique

The intrinsic ATPase activity of protein kinase C is catalyzed at the active site of the enzyme

Biochemistry ◽  
1992 ◽  
Vol 31 (25) ◽  
pp. 5905-5911 ◽  
Author(s):  
Nancy E. Ward ◽  
Catherine A. O'Brian
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atpase Activity ◽  
Active Site ◽  
Kinase C

Studies on the mechanism of action of a bilayer stabilizing inhibitor of protein kinase C: Cholesterylphosphoryldimethylethanolamine

1989 ◽  
Vol 9 (3) ◽  
pp. 315-328 ◽  
Author(s):  
Richard M. Epand ◽  
Alan R. Stafford ◽  
Remo Bottega ◽  
Eric H. Ball
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Active Site ◽  
Potent Inhibitor ◽  
Competitive Inhibition ◽  
Inhibition Kinetics ◽  
Kinase C ◽  
Triton X ◽  
Kinetics Of ◽  
Tryptic Hydrolysis

Cholesterylphosphoryldimethylethanolamine is a zwitterionic compound which is a good bilayer stabilizer. As has been found with many other compounds having these properties, cholesterylphosphoryldimethylethanolamine is found to be a potent inhibitor of protein kinase C in both vesicle and micelle assay systems. The kinetics of the inhibition in Triton X-100 micelles was non-competitive with respect to ATP, histone, diolein, phorbol ester and Ca2+. It has a Ki of about 30 μm. The inhibition kinetics as a function of phosphatidylserine concentration is more complex but suggestive of competitive inhibition. Cholesterylphosphoryldimethylethanolamine does not prevent the partitioning of protein kinase C into the membrane. This inhibitor lowers the Ca2+-phosphatidylserine-independent phosphorylation of protamine sulfate by protein kinase C and directly affects the catalytic segment of the enzyme generated by tryptic hydrolysis. Thus, this zwitterionic bilayer stabilizing inhibitor of protein kinase C both competes with the binding of phosphatidylserine as well as affects the active site of protein kinase C.

scholarly journals The active site substrate specificity of protein kinase C.

1994 ◽  
Vol 269 (7) ◽  
pp. 4839-4844
Author(s):  
Y.G. Kwon ◽  
M. Mendelow ◽  
D.S. Lawrence
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Substrate Specificity ◽  
Active Site ◽  
Kinase C

scholarly journals Active Site Inhibitors Protect Protein Kinase C from Dephosphorylation and Stabilize Its Mature Form

2011 ◽  
Vol 286 (33) ◽  
pp. 28922-28930 ◽  
Author(s):  
Christine M. Gould ◽  
Corina E. Antal ◽  
Gloria Reyes ◽  
Maya T. Kunkel ◽  
Ryan A. Adams ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Active Site ◽  
Mature Form ◽  
Kinase C

scholarly journals The active site substrate specificity of protein kinase C.

1994 ◽  
Vol 269 (14) ◽  
pp. 4839-4844
Author(s):  
Y.G. Kwon ◽  
M. Mendelow ◽  
D.S. Lawrence
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Substrate Specificity ◽  
Active Site ◽  
Kinase C
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