| Sphingomyelin phosphodiesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Crystal structure of sphingomyelinase from Bacillus cereus.[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 3.1.4.12 | ||||||||
| CAS no. | 9031-54-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Sphingomyelin phosphodiesterase (EC 3.1.4.12, also known as neutral sphingomyelinase, sphingomyelinase, or SMase; systematic name sphingomyelin cholinephosphohydrolase) is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses.[2]
- ^ PDB: 2ddt; Ago H, Oda M, Takahashi M, Tsuge H, Ochi S, Katunuma N, Miyano M, Sakurai J (June 2006). "Structural basis of the sphingomyelin phosphodiesterase activity in neutral sphingomyelinase from Bacillus cereus". J. Biol. Chem. 281 (23): 16157–67. doi:10.1074/jbc.M601089200. PMID 16595670.
- ^ Hannun YA, Obeid LM (July 2002). "The Ceramide-centric universe of lipid-mediated cell regulation: stress encounters of the lipid kind". J. Biol. Chem. 277 (29): 25847–50. doi:10.1074/jbc.R200008200. PMID 12011103.