- See also
- References
- External links
| Name = Sphingomyelin phosphodiesterase D
| EC_number = 3.1.4.41
| CAS_number = 54992-31-3
| IUBMB_EC_number = 3/1/4/41
| GO_code =
| image =
| width =
| caption = Crystal structure of Sphingomyelin phosphodiesterase D, class II phospholipase D from the recluse spider Loxosceles intermedia (from PDB entry {{PDB2|3RLH}} [1])
}}
Sphingomyelin phosphodiesterase D ({{EC number|3.1.4.41}}, sphingomyelinase D) is an enzyme of the sphingomyelin phosphodiesterase family with systematic name sphingomyelin ceramide-phosphohydrolase.[2][3] These enzymes catalyse the hydrolysis of sphingomyelin, resulting in the formation of ceramide 1-phosphate and choline:
sphingomyelin + H2Oceramide 1-phosphate + choline
or the hydrolysis of 2-lysophosphatidylcholine to give choline and 2-lysophosphatidate.
Sphingomyelin phosphodiesterase D activity is shared by enzymes with a wider substrate range, classified as phospholipases D or lipophosphodiesterase II {{EC number|3.1.4.4}}.[4]
Sphingomyelinases D are produced by some spiders in their venoms, by arthropods such as ticks, or pathogenic bacteria and fungi. Pathogenicity is expressed through different mechanisms, such as membrane destabilization, cell penetration, inflammation of the lungs and cutaneous lesions, common following spider bites.
See also
- Sphingomyelin phosphodiesterase
References
2. ^{{cite journal | vauthors = Carne HR, Onon EO | title = Action of Corynebacterium ovis exotoxin on endothelial cells of blood vessels | journal = Nature | volume = 271 | issue = 5642 | pages = 246–8 | date = January 1978 | pmid = 622164 | doi = 10.1038/271246a0 }}
3. ^{{cite journal | vauthors = Soucek A, Michalec C, Soucková A | title = Identification and characterization of a new enzyme of the group "phospholipase D" isolated from Corynebacterium ovis | journal = Biochimica et Biophysica Acta | volume = 227 | issue = 1 | pages = 116–28 | date = January 1971 | pmid = 5543581 | doi = 10.1016/0005-2744(71)90173-2 }}
4. ^{{cite journal | vauthors = Murakami MT, Fernandes-Pedrosa MF, Tambourgi DV, Arni RK | title = Structural basis for metal ion coordination and the catalytic mechanism of sphingomyelinases D | journal = The Journal of Biological Chemistry | volume = 280 | issue = 14 | pages = 13658–64 | date = April 2005 | pmid = 15654080 | doi = 10.1074/jbc.M412437200 }}
External links
- {{MeshName|Sphingomyelin+phosphodiesterase+D}}
- http://www.arachnoserver.org/toxincard.html?id=138
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