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Effects of nucleotides and divalent cations on phospholipase activity in Saccharomyces cerevisiae
1Institut für Pharmakologie und Toxikologie, Philipps-Universität Marburg, Federal Republic of Germany.
Archives of Microbiology
|January 1, 1989
Abstract:
Divalent cations activate the lysophospholipase and transacylase reactions catalyzed by the same enzymes in the yeast Saccharomyces cerevisiae. The activation was observed at neutral pH, but not at the pH optimum of lysophospholipase/transacylase, near 3.5. Adenine nucleotides, especially AMP and ADP, are strong inhibitors of the same group of enzymes. Half maximal inhibition by AMP was found at a concentration of about 20 microM. The inhibition by nucleotides in low concentrations is enhanced by divalent cations.