Sphingomyelinase
From Proteopedia
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<StructureSection load='1zwx' size='350' side='right' caption='Sphingomyelinase complex with glycerol and phosphate ion (PDB entry [[21zwx])' scene=''> | <StructureSection load='1zwx' size='350' side='right' caption='Sphingomyelinase complex with glycerol and phosphate ion (PDB entry [[21zwx])' scene=''> | ||
== Function == | == Function == | ||
| - | '''Sphingomyelinase''' (SMase) or '''sphingomyelin phosphodiesterase''' is a hydrolase involved in sphingolipid metabolism. It catalyzes the breakdown of sphingomyelin (SM) to phosphocholine and | + | '''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. | ||
| + | *'''Acid SMase-like phosphodiesterase 3B''' is a GPI-anchored protein with role in inflammatory processes and kidney disease<ref>PMID:27687724</ref>. | ||
| + | *'''Alkaline SMase''' hydrolyses sphingomyelin in the intestinal tract and bile<ref>PMID:16631405</ref>. | ||
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| + | See also [[Lipid signaling]]. | ||
== Disease == | == Disease == | ||
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*SMase | *SMase | ||
| + | **[[5uvg]] – hSMase catalytic domain – human<br /> | ||
**[[3rlh]], [[3rlg]] – SMase D (mutant) – ''Loxosceles intermedia''<br /> | **[[3rlh]], [[3rlg]] – SMase D (mutant) – ''Loxosceles intermedia''<br /> | ||
**[[1xx1]], [[2f9r]] – SMase I – ''Loxosceles laeta''<br /> | **[[1xx1]], [[2f9r]] – SMase I – ''Loxosceles laeta''<br /> | ||
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**[[2ddr]], [[2dds]], [[2ddt]] – BcSMase + cation – ''Bacillus cereus''<br /> | **[[2ddr]], [[2dds]], [[2ddt]] – BcSMase + cation – ''Bacillus cereus''<br /> | ||
**[[2uyr]] – BcSMase (mutant)<br /> | **[[2uyr]] – BcSMase (mutant)<br /> | ||
| - | **[[ | + | **[[7cne]] – SMase C – ''Streptomyces griseocarneus''<br /> |
| - | + | ||
*Acid SMase | *Acid SMase | ||
| + | **[[5jg8]], [[5i81]], [[5i8r]] – hSMase <br /> | ||
| + | **[[5i85]] – hSMase + phosphocholine<br /> | ||
**[[5fib]] – mSMase – mouse<br /> | **[[5fib]] – mSMase – mouse<br /> | ||
**[[5hqn]] – mSMase catalytic domain<br /> | **[[5hqn]] – mSMase catalytic domain<br /> | ||
**[[5fi9]] – mSMase + inhibitor<br /> | **[[5fi9]] – mSMase + inhibitor<br /> | ||
**[[5fic]] – mSMase + lipid<br /> | **[[5fic]] – mSMase + lipid<br /> | ||
| - | **[[5jg8]], [[5i81]], [[5i8r]] – hSMase <br /> | ||
| - | **[[5i85]] – hSMase + phosphocholine<br /> | ||
*Acid SMase-like phosphodiesterase | *Acid SMase-like phosphodiesterase | ||
| + | **[[5ebb]] – hSMase 3A<br /> | ||
| + | **[[5ebe]] – hSMase 3A + CMP<br /> | ||
**[[5fc1]], [[5fc7]], [[5fca]] – mSMase 3A<br /> | **[[5fc1]], [[5fc7]], [[5fca]] – mSMase 3A<br /> | ||
**[[5fcb]] – mSMase 3A + AMP<br /> | **[[5fcb]] – mSMase 3A + AMP<br /> | ||
**[[5fc6]] – mSMase 3A + AMPCP<br /> | **[[5fc6]] – mSMase 3A + AMPCP<br /> | ||
**[[5fc5]] – mSMase 3A + phosphocholine<br /> | **[[5fc5]] – mSMase 3A + phosphocholine<br /> | ||
| - | **[[5ebb]] – hSMase 3A<br /> | ||
| - | **[[5ebe]] – hSMase 3A + CMP<br /> | ||
**[[5kar]] – mSMase 3B<br /> | **[[5kar]] – mSMase 3B<br /> | ||
**[[5kas]] – mSMase 3B + phosphocholine<br /> | **[[5kas]] – mSMase 3B + phosphocholine<br /> | ||
Current revision
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3D structures of sphingomyelinase
Updated on 14-August-2024
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
- ↑ Duan RD. Alkaline sphingomyelinase: an old enzyme with novel implications. Biochim Biophys Acta. 2006 Mar;1761(3):281-91. Epub 2006 Mar 30. PMID:16631405 doi:10.1016/j.bbalip.2006.03.007
- ↑ 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
