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Ceramidase (CDase) is an enzyme that hydrolyzes the N-acyl linkage between a fatty acid and a sphingoid base in ceramide (Cer) and is widely distributed from bacteria to mammals. Cer comprises the hydrophobic portion of complex sphingolipids including sphingomyelin and glycosphingolipids. The most abundant sphingoid base in mammalian tissues is sphingosine (Sph), which has a trans-double bond between the C4 and C5 positions, and Sph can be phosphorylated by Sph kinases and converted to Sph 1-phosphate (S1P). Cer, Sph, and S1P have been shown to function as lipid signaling molecules that regulate various signal transduction systems. Sph cannot be synthesized via the de novo sphingolipid biosynthesis pathway; that is, the formation of the C4–C5 trans-double bond by dihydroceramide desaturase, DES1, occurs after N-acylation of dihydrosphingosine by Cer synthases, and...
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