1993
DOI: 10.1021/bi00095a015 View full text |Buy / Rent full text
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Abstract: The inhibition by melittin, a model calmodulin-binding peptide, of phosphorylase kinase, which contains an intrinsic calmodulin subunit, has been characterized in detail. The inhibition was competitive with respect to phosphorylase b for both the phosphorylase kinase holoenzyme and its isolated catalytic gamma-subunit (minus calmodulin), and the ratios of the Km for phosphorylase to the Ki for melittin were similar for both forms of the kinase. These findings indicate that inhibition of the phosphorylase kinas… Show more

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“…Thus, electrostatic repulsions between the positively charged N terminus of this peptide and the basic residues of melittin may lessen or prevent such interactions from occurring and, in turn, eliminate the inhibitory activity. Melittin is known to bind to a number of proteins such as calmodulin (34), troponin C (35), and phosphorylase kinase (36). In particular, it has been reported that melittin binds to calmodulin (34) or troponin C (35) through the exposed hydrophobic surfaces.…”
Section: Discussionmentioning
“…* * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * --388 * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * --272 * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * * 212 The proposed mode of regulation of mammalian CaM kinases involves binding of CaM to such a basic amphipathic s-helical motif, displacing an overlapping autoinhibitory pseudosubstrate sequence from the active site [5,18,28,40]. In vitro studies with recombinant CDPKs from soybean [31] and Arabidopsis [2], in conjunction with the finding that basic polypeptides can inhibit plant calcium-dependent protein kinases [9,29], have provided initial evidence that these regions bind the calmodulin-like domain and also contain an autoinhibitory pseudosubstrate motif.…”
Section: L H R S Y S T E a D V W S I G V I S Y I L L C G S R P F W mentioning
“…A number of studies on the interactions of melittin with both prokaryotic and eukaryotic cells have shown that the peptide can interact with a range of cellular proteins which are linked with tight junction regulation and permeability. These include binding to calmodulin (18), inhibition of the sodium-potassium, hydrogen-potassium, and calcium ATPase pumps (19,20), as well as protein kinase C (PKC) (21), phosphorylase kinase (22), troponin C (18), and adenylate cyclase (23) among others.…”
Section: Introductionmentioning
“…The use of SCLs composed entirely of D-amino acid peptides showed that proteins or protein-like complexes that bind to a range of peptide ligands (e.g. melittin is known to bind to calmodulin (Itakura and Iio, 1992), troponin C (Steiner and Norris, 1987), and phosphorylase kinase (Paudel et al, 1993)) might also be able to bind all-D-amino acid peptides. In a similar manner, calmodulin was recently reported to be able to interact with amphiphilic peptides composed only of Damino acids (Fisher et al, 1994).…”
Section: Resultsmentioning
“…Binding of Ca^^-calmodulin to a and |3 (39) activates phosphorylase kinase (30,40 178,41). The binding of exogenous calmodulin, termed 5', to a and P is Ca^-^dependent, as it can be inhibited by trifluoperazine, and calmodulin binding peptides melittin and mastoparan (42). Protein kinase A and calmodulin complement each other in the regvilation of phosphorylase kinase activity (43).…”
Section: Roles Of Subunits a And The Regulatory Subunitsmentioning