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Enzymatic Hydrolysis of Sphingolipids

I. HYDROLYSIS AND SYNTHESIS OF CERAMIDES BY AN ENZYME FROM RAT BRAIN

From the ¹ From the Department of Biochemistry, Hebrew University-Hadassah Medical School, Jerusalem, Israel

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.

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