Activation of a cyclic nucleotide phosphodiesterase and of a protein kinase by chemically modified calmodulin.
1. Several calmodulin derivatives prepared by chemical modification of lysine residues were tested using bovine heart cyclic nucleotide phosphodiesterase and wheat germ calmodulin-dependent protein kinase. 2. The effect of chemical modification on the activation capacity of calmodulin for the two studied enzymes was different. 3. This was particularly noticeable in the case of alkylated derivatives which exhibited a higher affinity than native calmodulin towards phosphodiesterase but a lower affinity towards protein kinase. 4. The efficiency of these derivatives (maximal activation) was higher than that of native calmodulin in relation with the protein kinase.
Tertrin-Clary
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CNRS, Hormones Polypeptidiques, Gif sur Yvette, France.
Chenut
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MC
de la Llosa
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P
D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000378:metabolism*; D000478:Alkylation; D000818:Animals; D002147:Calmodulin / Q000031:analogs & derivatives / Q000494:pharmacology*; D004789:Enzyme Activation / Q000187:drug effects; D066298:In Vitro Techniques; D008297:Male; D010761:Phosphorus Radioisotopes; D011494:Protein Kinases / Q000378:metabolism*; D012756:Sheep; D014908:Triticum / Q000201:enzymology
D002147:Calmodulin; D010761:Phosphorus Radioisotopes; D011494:Protein Kinases; D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases