Enzymatic Hydrolysis of Sphingolipids

作者：Shimon Gátt · 发表于：Journal of Biological Chemistry · 年份：1966 · DOI：10.1016/s0021-9258(18)99832-7 · 被引用次数：204 · 研究领域：Sphingolipid Metabolism and Signaling、Lipid Membrane Structure and Behavior、Lipid metabolism and biosynthesis

Abstract An enzyme was extracted from rat brain and purified about 100-fold. It catalyzed a reversible reaction in which the amide bond of ceramide (N-acylsphingosine) was either hydrolyzed or synthesized. The hydrolysis of ceramide to sphingosine and fatty acid had a pH optimum of 4.8, required cholate or taurocholate, and was inhibited by both sphingosine and fatty acid. N-Palmitoyl-, N-stearoyl-, and N-oleylsphingosine or dihydrosphingosine were hydrolyzed, but N-acetylsphinogsine, N-lignoceryldihydrosphingosine, cerebroside, and sphingomyelin did not serve as substrates in this reaction. The synthesis of ceramide from sphingosine and fatty acid also had a pH optimum of 4.8 and required cholate. It was not inhibited by fatty acid at pH 8, but was inhibited at pH 5 by fatty acid concentrations greater than 3 x 10-4 M.