Effects of nucleotides and divalent cations on phospholipase activity in Saccharomyces cerevisiae.
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.
Witt
W
W
Institut für Pharmakologie und Toxikologie, Philipps-Universität Marburg, Federal Republic of Germany.
Hampel
P
P
Böcker
K
K
Mertsching
A
A
D000217:Acyltransferases / Q000378:metabolism; D000244:Adenosine Diphosphate / Q000494:pharmacology; D000249:Adenosine Monophosphate / Q000494:pharmacology; D002122:Calcium Chloride / Q000494:pharmacology*; D002413:Cations, Divalent / Q000494:pharmacology; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D008245:Lysophospholipase / Q000378:metabolism; D008274:Magnesium / Q000494:pharmacology*; D015636:Magnesium Chloride; D009705:Nucleosides / Q000494:pharmacology; D009711:Nucleotides / Q000494:pharmacology*; D010740:Phospholipases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology*
D002413:Cations, Divalent; D009705:Nucleosides; D009711:Nucleotides; D015636:Magnesium Chloride; D000249:Adenosine Monophosphate; D000244:Adenosine Diphosphate; D000217:Acyltransferases; D010740:Phospholipases; D008245:Lysophospholipase; D008274:Magnesium; D002122:Calcium Chloride