Acid ceramidase hydrolyses ceramide into sphingosine and free fatty acid (lysosome)

Stable Identifier
R-HSA-1606602
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Acid ceramidase (ASAH1) is a lysosomal enzyme that catalyses the hydrolysis of ceramide to sphingosine and free fatty acid. It functions as a heterodimer of one alpha and one beta subunit (Bernardo et al. 1995). Defects in ASAH1 are the cause of Farber lipogranulomatosis (FL) (MIM:228000), also called Farber disease (FD) (Zhang et al. 2000, Koch et al. 1996).

Literature References
PubMed ID Title Journal Year
8955159 Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease

Koch, J, Gärtner, S, Li, CM, Quintern, LE, Bernardo, K, Levran, O, Schnabel, D, Desnick, RJ, Schuchman, EH, Sandhoff, K

J Biol Chem 1996
10993717 Human acid ceramidase gene: novel mutations in Farber disease

Zhang, Z, Mandal, AK, Mital, A, Popescu, N, Zimonjic, D, Moser, A, Moser, H, Mukherjee, AB

Mol Genet Metab 2000
7744740 Purification, characterization, and biosynthesis of human acid ceramidase

Bernardo, K, Hurwitz, R, Zenk, T, Desnick, RJ, Ferlinz, K, Schuchman, EH, Sandhoff, K

J Biol Chem 1995
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
N-acylsphingosine amidohydrolase activity of ASAH1 [lysosomal lumen]
Physical Entity
Activity
Orthologous Events
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