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J. Biol. Chem., Vol. 260, Issue 21, 11503-11507, 09, 1985
RS Turner, BE Kemp, HD Su and JF Kuo
The substrate specificity of phospholipid/Ca2+-dependent protein kinase
(protein kinase C) was studied using synthetic peptides, in particular
those corresponding to the amino acid sequence around serine 115 in bovine
myelin basic protein (MBP). It was found that MBP (104-118) and MBP
(104-123) were substrates for the enzyme, with apparent Km values of 14 and
10 microM, respectively. Neither MBP (111-118) nor MBP (111- 123) were
phosphorylated, indicating that an additional segment of sequence extending
toward the N terminus, but not toward the C terminus, was essential for the
substrate activity of the peptides. Of the alanine-substituted analogs
examined, [Ala 105] MBP (104-118) was comparable to the parent peptide,
whereas [Ala 107] MBP (104-118) and [Ala 113] MBP-(104-118) were much
poorer substrates. These findings indicated that lysine 105 was not
essential, but both arginine 107 and arginine 113 were important
specificity determinants. Initial studies revealed that [Ala 113] MBP
(104-118) inhibited phosphorylation by the enzyme of the parent peptide
and, to a lesser extent, the intact MBP(1- 170). Serine 115 was the only
site phosphorylated in the analog peptides [Ala 105] MBP (104-118) and [Ala
107]MBP (104-118). In the parent peptide, serine 115 was the initial site
of phosphorylation but after prolonged phosphorylation other sites became
phosphorylated (serine 110 and/or serine 112), further supporting the
concept that arginine residues act as essential substrate specificity
determinants for phospholipid/Ca2+-dependent protein kinase.
Substrate specificity of phospholipid/Ca2+-dependent protein kinase as probed with synthetic peptide fragments of the bovine myelin basic protein
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