Characterization of Synthetic Peptide Substrates for p34cdc2 Protein Kinase

1991 ◽  
Vol 45 (4) ◽  
pp. 391-400 ◽  
Author(s):  
Daniel R. Marshak ◽  
Mark T. Vandenberg ◽  
Young Seuk Bae ◽  
Ii Je Yu
Keyword(s):  
Protein Kinase ◽  
Synthetic Peptide ◽  
Peptide Substrates

scholarly journals Differential responses of cyclic GMP-dependent and cyclic AMP-dependent protein kinases to synthetic peptide inhibitors

1983 ◽  
Vol 213 (1) ◽  
pp. 159-164 ◽  
Author(s):  
D B Glass
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Protein Kinases ◽  
Cyclic Gmp ◽  
Synthetic Peptide ◽  
Peptide Inhibitors ◽  
Catalytic Subunit ◽  
Dependent Protein Kinase ◽  
Peptide Substrates ◽  
Dependent Protein

The peptide Arg-Lys-Arg-Ala-Arg-Lys-Glu was synthesized and tested as an inhibitor of cyclic GMP-dependent protein kinase. This synthetic peptide is a non-phosphorylatable analogue of a substrate peptide corresponding to a phosphorylation site (serine-32) in histone H2B. The peptide was a competitive inhibitor of cyclic GMP-dependent protein kinase with respect to synthetic peptide substrates, with a Ki value of 86 microM. However, it did not inhibit phosphorylation of intact histones by cyclic GMP-dependent protein kinase under any conditions tested. Arg-Lys-Arg-Ala-Arg-Lys-Glu competitively inhibited the phosphorylation of either peptides or histones by the catalytic subunit of cyclic AMP-dependent protein kinase, with similar Ki values (550 microM) for both of these substrates. The peptide Leu-Arg-Arg-Ala-Ala-Leu-Gly, which was previously reported to be a selective inhibitor of both peptide and histone phosphorylation by cyclic AMP-dependent protein kinase, was a poor inhibitor of cyclic GMP-dependent protein kinase acting on peptide substrates (Ki = 800 microM), but did not inhibit phosphorylation of histones by cyclic GMP-dependent protein kinase. The selectivity of these synthetic peptide inhibitors toward either cyclic GMP-dependent or cyclic AMP-dependent protein kinases is probably based on differences in the determinants of substrate specificity recognized by these two enzymes. It is concluded that histones interact differently with cyclic GMP-dependent protein kinase from the way they do with the catalytic subunit of cyclic AMP-dependent protein kinase.

scholarly journals Characterization of Endoplasmic Reticulum-Localized UDP-d-Galactose: Hydroxyproline O-Galactosyltransferase Using Synthetic Peptide Substrates in Arabidopsis

2009 ◽  
Vol 152 (1) ◽  
pp. 332-340 ◽  
Author(s):  
Takuji Oka ◽  
Fumie Saito ◽  
Yoh-ichi Shimma ◽  
Takehiko Yoko-o ◽  
Yoshiyuki Nomura ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Synthetic Peptide ◽  
Peptide Substrates

Studies with synthetic peptide substrates derived from the neuronal protein neurogranin reveal structural determinants of potency and selectivity for protein kinase C

Biochemistry ◽  
1993 ◽  
Vol 32 (4) ◽  
pp. 1032-1039 ◽  
Author(s):  
Shu Jen Chen ◽  
Eric Klann ◽  
Morganne C. Gower ◽  
Craig M. Powell ◽  
J. Suzanne Sessoms ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Synthetic Peptide ◽  
Structural Determinants ◽  
Peptide Substrates ◽  
Neuronal Protein ◽  
Kinase C
Sign in / Sign up

Export Citation Format

Share Document