|
|
| Line 5: |
Line 5: |
| *'''Acid SMase-like phosphodiesterase 3A''' hydrolyzes nucleotides triphosphates and diphosphates. | | *'''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>. | | *'''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>. |
|
| |
|
| See also [[Lipid signaling]]. | | See also [[Lipid signaling]]. |
Latest revision as of 07:18, 14 August 2024
| 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.
- Acid SMase-like phosphodiesterase 3B is a GPI-anchored protein with role in inflammatory processes and kidney disease[2].
- Alkaline SMase hydrolyses sphingomyelin in the intestinal tract and bile[3].
See also Lipid signaling.
Disease
Mutations in acid SMase are found in patients with Niemann-Pick disease[4].
- ↑ 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:https://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:https://dx.doi.org/10.1016/j.jpeds.2006.06.034
|
3D structures of sphingomyelinase
Updated on 14-August-2024
{"openlevels":0}
- SMase
- Ceramide – hSMase catalytic domain – human
- Lipid signaling, 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)
- 7cne – SMase C – Streptomyces griseocarneus
- Acid SMase
- Acid SMase-like phosphodiesterase
- 5ebb – hSMase 3A
- 5ebe – hSMase 3A + CMP
- 5fc1, 5fc7, 5fca – mSMase 3A
- 5fcb – mSMase 3A + AMP
- 5fc6 – mSMase 3A + AMPCP
- 5fc5 – mSMase 3A + phosphocholine
- 5kar – mSMase 3B
- 5kas – mSMase 3B + phosphocholine
- Alkaline SMase
- 5udy – hSMase
- 5tcd – hSMase + phosphocholine
References
