Calcium-independent activation of two plant leaf calcium-regulated protein kinases by unsaturated fatty acids.
Two soluble Ca2+-dependent protein kinases from silver beet leaves (enzymes I and II) can be resolved from each other by chromatography on DEAE-cellulose. Enzyme II is substantially activated by arachidonic, oleic and linoleic acids in the absence of Ca2+ but not at high Ca2+ concentrations. Stearic and arachidic acids do not substantially activate either enzyme at low free Ca2+. Enzyme I differs from enzyme II in exhibiting a much lower degree of Ca2+-independent activation by unsaturated fatty acids.
Klucis
E
E
Department of Biochemistry, La Trobe University, Bundoora, Victoria, Australia.
Polya
G M
GM
D002118:Calcium / Q000502:physiology*; D004789:Enzyme Activation; D005231:Fatty Acids, Unsaturated / Q000502:physiology*; D066298:In Vitro Techniques; D018521:Plant Physiological Phenomena; D011494:Protein Kinases / Q000378:metabolism*; D013379:Substrate Specificity
D005231:Fatty Acids, Unsaturated; D011494:Protein Kinases; D002118:Calcium