Summary: The activity of trehalase in a crude extract of dormant spores increased 10- to 20-fold during incubation in the presence of cyclic AMP and ATP. A phosphorylation of the enzyme was probably involved, as a more pronounced activation was obtained when cyclic AMP was replaced by the catalytic subunit of beef heart protein kinase. The γ-thio derivative of ATP could replace ATP in the activation but was quantitatively less effective. The effective concentrations of cyclic AMP and ATP were comparable to their likely intracellular concentrations; thus phosphorylation could be the mechanism of trehalase activation during the activation of dormant spores by heat or acetate.


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