Sphingomyelinase
From Proteopedia
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{{STRUCTURE_1zwx| PDB=1zwx | SIZE=400| SCENE= |right|CAPTION=Sphingomyelinase complex with glycerol and phosphate ion [[1zwx]] }} | {{STRUCTURE_1zwx| PDB=1zwx | SIZE=400| SCENE= |right|CAPTION=Sphingomyelinase complex with glycerol and phosphate ion [[1zwx]] }} | ||
| - | + | == Function == | |
'''Sphingomyelinase''' (SMase) 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. | '''Sphingomyelinase''' (SMase) 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. | ||
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| + | == Disease == | ||
| + | Mutations in acid SMase are found in patients with Niemann-Pick disease<ref>PMID:17011332</ref>. | ||
==3D structures of sphingomyelinase== | ==3D structures of sphingomyelinase== | ||
Revision as of 08:51, 31 August 2016
Contents |
Function
Sphingomyelinase (SMase) 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.
Disease
Mutations in acid SMase are found in patients with Niemann-Pick disease[2].
3D structures of sphingomyelinase
Updated on 31-August-2016
3rlh, 3rlg – SMase D (mutant) – Loxosceles intermedia
1xx1, 2f9r – SMase I – Loxosceles laeta
1zwx – SMase C – Listeria ivanovii
2ddr, 2dds, 2ddt – BcSMase + cation – Bacillus cereus
2uyr – BcSMase (mutant)
3wcx – SMase C – Streptomyces griseocarneus
References
- ↑ Chatterjee S. Neutral sphingomyelinase: past, present and future. Chem Phys Lipids. 1999 Nov;102(1-2):79-96. PMID:11001563
- ↑ 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
