Sphingomyelin phosphodiesterase (SMPD1) hydrolyses sphingomyelin to ceramide (lysosome)

Stable Identifier
Reaction [transition]
Homo sapiens
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Sphingomyelin phosphodiesterase (SMPD1), also called acid sphingomyelinase (ASM), is a lysosomal phosphodiesterase that hydrolyses sphingomyelin to ceramide and phosphocholine (Schuchman et al. 1991, Schuchman et al. 1992). Defects in SMPD1 are the cause of two types of Niemann-Pick disease. Type A (NPDA, Niemann-Pick disease classical infantile form) (MIM:257200) (Ferlinz et al. 1991) and type B (NPDB, Niemann-Pick disease visceral form) (MIM:607616) (Rodriguez-Pascau et al. 2009).

Literature References
PubMed ID Title Journal Year
1718266 Molecular basis of acid sphingomyelinase deficiency in a patient with Niemann-Pick disease type A

Ferlinz, K, Hurwitz, R, Sandhoff, K

Biochem Biophys Res Commun 1991
19405096 Identification and characterization of SMPD1 mutations causing Niemann-Pick types A and B in Spanish patients

Rodríguez-Pascau, L, Gort, L, Schuchman, EH, Vilageliu, L, Grinberg, D, Chabás, A

Hum Mutat 2009
1840600 Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs

Schuchman, EH, Suchi, M, Takahashi, T, Sandhoff, K, Desnick, RJ

J Biol Chem 1991
1740330 Structural organization and complete nucleotide sequence of the gene encoding human acid sphingomyelinase (SMPD1)

Schuchman, EH, Levran, O, Pereira, LV, Desnick, RJ

Genomics 1992
Participant Of
Catalyst Activity
Catalyst Activity
sphingomyelin phosphodiesterase activity of SMPD1 [lysosomal lumen]
Physical Entity
Orthologous Events
Cross References
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