Evaluation of adenosine 5'-hexadecylphosphate as an inhibitor of acyl-CoA synthetase isozyme functional for phospholipid reconstitution in the yeast Saccharomyces cerevisiae
2001
Nakayama, K. (Osaka City Univ. (Japan)) | Tanaka, T.
Adenosine 5'-hexadecylphosphate (AMPC16) is a mimic of palmitoyl-AMP, a transient intermediate of the acyl-CoA synthetic reaction, and thus could effectively inhibit the activity of palmitoyl-CoA synthetase of Saccharomyces cerevisiae. AMPC16 inhibited the cellular incorporation of [sup3 H]palmitic acid into phospholipids, in which such an inhibition was most significantly detected in the fraction containing both phosphatidylinositol (PI) and phosphatidylserine (PS). A pulsechase experiment revealed the loss of PI and PS accompanied with accumulation of free fatty acids in AMPC16-treated cells. AMPC16-induced events suggested that Faalp, the major acyl-CoA synthetase isozyme, is functional for phospholipid reconstitution in the exponential growth phase.
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