Abstract
Ceramide, composed of a fatty acid and a sphingoid base linked by an N-acyl linkage, is the common lipid moiety of glycosphingoslipids (GSLs). Ceramide is synthesized in the ER, from where it is transported to the Golgi apparatus, and glycosylated in a stepby- step manner by various glycosyltransferases. After recycling from plasma membranes and intracellular organella, GSLs are finally sorted into the lysosomes where they are degraded by various exoglycosidases and ceramidase with the aid of corresponding activator proteins. Ceramidase is an enzyme capable of hydrolyzing the N-acyl linkage between a fatty acid and a sphingoid base in a free ceramide. Cermaidase can be classi- fied into three groups (acid, neutral, and alkaline enzymes) depending on their pH optima. It is worth noting that the three types of ceramidase are completely different in primary structure, suggesting that the isotypes of the enzyme are derived from different ancestral genes. This section deals with ceramidases and related enzymes. The action modes of enzymes described in this section are shown in Fig. 1.
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References
Furusato M, Sueyoshi N, Mitsutake S, Sakaguchi K, Kita K, Okino N, Ichinose S, Omori A, Ito M (2002) Molecular cloning and characterization of sphingolipid ceramide N-deacylase from a marine bacterium, Shewanella alga G8.. J Biol Chem 277:17300–17307
Horibata Y, Sakaguchi K, Okino N, Iida H, Inagaki M, Fujisawa T, Hama Y, Ito M (2004) Unique catabolic pathway of glycosphingolipids in a hydrozoan, Hydra magnipapillata, involving endoglycoceramidase. J Biol Chem 279:33379–33389
Ishibashi Y, Nakasone T, Kiyohara M, Horibata Y, Sakaguchi K, Hijikata A, Ichinose S, Omori A, Yasui Y, Imamura A, Ishida H, Kiso M, Okino N, Ito M (2007) A novel endoglycoceramidase hydrolyzes oligogalactosylceramides to produce galactooligosaccharides and ceramides. J Biol Chem 282:11386–11396
Okino N, Ito M (2007) Ceramidase enhances phospholipase C-induced hemolysis by Pseudomonas aeeruginosa. J Biol Chem 282:6021–6030
Tani M, Iida H, Ito M (2003) O-glycosylation of mucin-like domain retains the neutral ceramidase on the plasma membranes as a type II integral membrane protein. J Biol Chem 278:10523–10530
Yoshimura Y, Tani M, Okino N, Iida H, Ito M (2004) Molecular cloning and functional analysis of zebrafish neutral ceramidase. J Biol Chem 279:44012–44022
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Ito, M. (2008). Ceramidase and Related Enzymes. In: Taniguchi, N., Suzuki, A., Ito, Y., Narimatsu, H., Kawasaki, T., Hase, S. (eds) Experimental Glycoscience. Springer, Tokyo. https://doi.org/10.1007/978-4-431-77924-7_5
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DOI: https://doi.org/10.1007/978-4-431-77924-7_5
Publisher Name: Springer, Tokyo
Print ISBN: 978-4-431-77923-0
Online ISBN: 978-4-431-77924-7
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