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J. Biol. Chem., Vol. 261, Issue 18, 8140-8145, 06, 1986
DK Blumenthal, K Takio, RS Hansen and EG Krebs
Calmodulin-dependent protein phosphatase purified from bovine cardiac
muscle catalyzed the rapid dephosphorylation of Ser-95 of bovine cardiac
cAMP-dependent protein kinase regulatory subunit (RII). The kinetic
constants determined for the reaction (Km = 20 microM; Vmax = 2 mumol min-1
mg-1) are comparable to those determined for other good substrates of this
phosphatase. Because little is known about the determinants of substrate
specificity for the calmodulin-dependent phosphatase, various
phosphopeptides were used to investigate the structural features important
for substrate recognition. Limited proteolysis of phospho-RII with trypsin
and chymotrypsin yielded fragments (residues 93-400 and 91-400,
respectively) that were poor substrates, whereas digestion with
Staphylococcal aureus V8 protease produced three phosphopeptides that were
all dephosphorylated as rapidly as intact RII. The sequence of the shortest
phosphopeptide produced by S. aureus V8 protease was determined by sequence
analysis to be
Asp-Leu-Asp-Val-Pro-Ile-Pro-Gly-Arg-Phe-Asp-Arg-Arg-Val-Ser-Val-
Cys-Ala-Glu, corresponding to residues 81-99 of RII. Synthetic
phosphopeptides corresponding to residues 81-99, 85-99, 90-99, and 91- 99
were prepared to determine the minimum sequence necessary for substrate
recognition. Only the 19-residue peptide (81-99) was dephosphorylated with
kinetics comparable to RII (Km = 26 microM, Vmax = 1.7 mumol min-1 mg-1).
Structural analysis of this peptide indicates that an amphipathic
beta-sheet structure may be an important structural determinant for some
substrates of the calmodulin-dependent phosphatase.
Dephosphorylation of cAMP-dependent protein kinase regulatory subunit (type II) by calmodulin-dependent protein phosphatase. Determinants of substrate specificity
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