Sphingomyelinase
From Proteopedia
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== Function == | == Function == | ||
'''Sphingomyelinase''' (SMase) or '''sphingomyelin phosphodiesterase''' is a hydrolase involved in sphingolipid metabolism. It catalyzes the breakdown of sphingomyelin (SM) to phosphocholine and [[Ceramide]]<ref>PMID:11001563</ref>. 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<ref>PMID:27687724</ref>. | '''Sphingomyelinase''' (SMase) or '''sphingomyelin phosphodiesterase''' is a hydrolase involved in sphingolipid metabolism. It catalyzes the breakdown of sphingomyelin (SM) to phosphocholine and [[Ceramide]]<ref>PMID:11001563</ref>. 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<ref>PMID:27687724</ref>. | ||
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| + | See also [[Lipid signaling]]. | ||
== Disease == | == Disease == | ||
Revision as of 08:22, 15 January 2023
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3D structures of sphingomyelinase
Updated on 15-January-2023
References
- ↑ Chatterjee S. Neutral sphingomyelinase: past, present and future. Chem Phys Lipids. 1999 Nov;102(1-2):79-96. PMID:11001563
- ↑ 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
- ↑ 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
