SMPD1 hydrolyzes SPHM

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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
19405096 Identification and characterization of SMPD1 mutations causing Niemann-Pick types A and B in Spanish patients

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

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

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

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

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

Genomics 1992
Catalyst Activity

sphingomyelin phosphodiesterase activity of SMPD1 [lysosomal lumen]

Orthologous Events
Cite Us!