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Chemistry and Physics of Lipids, 2016
The topic of ceramidases has experienced an enormous boost during the last few years. Ceramidases catalyze the degradation of ceramide to sphingosine and fatty acids. Ceramide is not only the central hub of sphingolipid biosynthesis and degradation, it is also a key molecule in sphingolipid signaling, promoting differentiation or apoptosis.
Essa M, Saied, Christoph, Arenz
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The topic of ceramidases has experienced an enormous boost during the last few years. Ceramidases catalyze the degradation of ceramide to sphingosine and fatty acids. Ceramide is not only the central hub of sphingolipid biosynthesis and degradation, it is also a key molecule in sphingolipid signaling, promoting differentiation or apoptosis.
Essa M, Saied, Christoph, Arenz
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Acid ceramidase and human disease
Biochimica Et Biophysica Acta - Biomembranes, 2006 Acid ceramidase (N-acylsphingosine deacylase, EC 3.5.1.23; AC) is the lipid hydrolase responsible for the degradation of ceramide into sphingosine and free fatty acids within lysosomes. The enzymatic activity was first identified over four decades ago, and is deficient in the inherited lipid storage disorder, Farber Lipogranulomatosis (Farber disease).
Park, Jae-Ho, Schuchman, Edward H.
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Alkaline ceramidase family: The first two decades
Cellular Signalling, 2021Ceramidases are a group of enzymes that catalyze the hydrolysis of ceramide, dihydroceramide, and phytoceramide into sphingosine (SPH), dihydrosphingosine (DHS), and phytosphingosine (PHS), respectively, along with a free fatty acid. Ceramidases are classified into the acid, neutral, and alkaline ceramidase subtypes according to the pH optima for their
Cungui Mao
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The molecular medicine of acid ceramidase
Biological Chemistry, 2015Abstract Acid ceramidase (N-acylsphingosine deacylase, EC 3.5.1.23; AC) is the lipid hydrolase responsible for the degradation of ceramide into sphingosine and free fatty acids within lysosomes. The enzymatic activity was first identified over four decades ago and is deficient in two rare inherited disorders, Farber lipogranulomatosis (Farber disease ...
Michael, Frohbergh +2 more
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Ceramidase Deficiency in Farber's Disease (Lipogranulomatosis)
Science, 1972Ceramidase activity could not be demonstrated in the kidney and cerebellum from a deceased patient with Farber's disease, whereas the activities of six control acid hydrolase enzymes appeared normal. This enzyme defect presumably accounts for the accumulation that has been described in two patients and may represent the biochemical basis of this ...
M, Sugita, J T, Dulaney, H W, Moser
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Acid and alkaline ceramidases of rat tissues
Biochemistry and Cell Biology, 1986Ceramidase (N-acylsphingosine deacylase) was measured in rat tissue homogenates with N-[1-14C]oleoyl- and N-[9,10-3H]palmitoyl-sphingosine. Two activities were observed with pH optima of approximately 5 and 8. The activity at pH 8 exceeded that at pH 5 in all tissues and tissue areas examined, and both activities decreased in the following order ...
M W, Spence, S, Beed, H W, Cook
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Properties of acid ceramidase from human spleen
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1989We have characterised ceramidase activity in extracts of human spleen from control subjects and from patients with Gaucher disease. In Triton X-100 extracts of control spleens, a broad pH optimum of pH 3.5-5.0 was found; no ceramidase activity was detectable at neutral or alkaline pH.
B J, Al +5 more
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Ceramidase and Signal Transduction
1997The deacylation of ceramide to form sphingosine in cells is the result of the activity of a group of enzymes referred to as the ceramidases (EC 3.5.1.23). There is a lysosomal form with an acidic pH optimum, a form with an alkaline pH optimum that may be associated with the plasma membrane and a form with a neutral pH optimum with a more limited tissue
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