Sphingomyelinase

From Proteopedia

Revision as of 17:48, 11 November 2020

spinqualitylabelsall models Sphingomyelinase complex with glycerol and phosphate ion (PDB entry [[21zwx]) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Sphingomyelinase (SMase) or sphingomyelin phosphodiesterase is a hydrolase involved in sphingolipid metabolism. It catalyzes the breakdown of sphingomyelin (SM) to phosphocholine and ceramide[1]. The SMase is classified into 5 types according to their pH dependence and cation dependence. Acid SMase-like phosphodiesterase is a paralog of acid SMase and thus though related by gene duplication has different functions. Acid SMase-like phosphodiesterase 3A hydrolyzes nucleotides triphosphates and diphosphates while Acid SMase-like phosphodiesterase 3B is a GPI-anchored protein with role in inflammatory processes and kidney disease[2]. Disease Mutations in acid SMase are found in patients with Niemann-Pick disease[3].

3D structures of sphingomyelinase

Updated on 11-November-2020

References

1. ↑ Chatterjee S. Neutral sphingomyelinase: past, present and future. Chem Phys Lipids. 1999 Nov;102(1-2):79-96. PMID:11001563
2. ↑ Gorelik A, Heinz LX, Illes K, Superti-Furga G, Nagar B. Crystal Structure of the Acid Sphingomyelinase-Like Phosphodiesterase SMPDL3B Provides Insights into Determinants of Substrate Specificity. J Biol Chem. 2016 Sep 28. pii: jbc.M116.755801. PMID:27687724 doi:http://dx.doi.org/10.1074/jbc.M116.755801
3. ↑ Wasserstein MP, Aron A, Brodie SE, Simonaro C, Desnick RJ, McGovern MM. Acid sphingomyelinase deficiency: prevalence and characterization of an intermediate phenotype of Niemann-Pick disease. J Pediatr. 2006 Oct;149(4):554-9. PMID:17011332 doi:http://dx.doi.org/10.1016/j.jpeds.2006.06.034