Inhibition by alpha factor of the glucose-induced activation of regulatory trehalase in Saccharomyces cerevisiae.

The enzyme activity of the regulatory trehalase (alpha, alpha-trehalose glycohydrolase; EC 3.2.1.28) in stationary-phase cells of Saccharomyces cerevisiae increased upon addition of glucose to cell suspensions. Such increase was temporarily retarded in the presence of alpha factor in the medium. The transient inhibition required the joined action of the pheromone-like factor and the protease inhibitor N-alpha-p-tosyl-L-lysine chloromethyl ketone. The inhibition of the glucose-induced activation of trehalase by alpha factor lends support to the involvement of adenosine 3',5'-cyclic monophosphate in the enzyme activation in vivo.