A novel enzyme that catalyzes the esterification of N-acetylsphingosine: metabolism of C2-ceramides
A Abe, JA Shayman, NS Radin - Journal of Biological Chemistry, 1996 - ASBMB
A unique transacylase that catalyzes esterification of a short chain ceramide, N-
acetylsphingosine, was found in Madin-Darby canine kidney cell and mouse tissue
homogenates. It esterified the hydroxyl group at the carbon-1 position of the ceramide. The
enzyme has a pH optimum of 4.2 and a K m of 9.4 µM for N-acetylsphingosine at pH 4.5. The
transacylase activity is independent of free fatty acid or acyl-CoA and instead uses the 2-acyl
group of phosphatidylethanolamine or phosphatidylcholine. The transacylase activity in the …
acetylsphingosine, was found in Madin-Darby canine kidney cell and mouse tissue
homogenates. It esterified the hydroxyl group at the carbon-1 position of the ceramide. The
enzyme has a pH optimum of 4.2 and a K m of 9.4 µM for N-acetylsphingosine at pH 4.5. The
transacylase activity is independent of free fatty acid or acyl-CoA and instead uses the 2-acyl
group of phosphatidylethanolamine or phosphatidylcholine. The transacylase activity in the …
