Sphingomyelin phosphodiesterase D
| Sphingomyelin phosphodiesterase D | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.1.4.41 | ||||||||
| CAS number | 54992-31-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Sphingomyelin phosphodiesterase D (EC 3.1.4.41, sphingomyelinase D) is an enzyme of the sphingomyelin phosphodiesterase family with systematic name sphingomyelin ceramide-phosphohydrolase.[1][2] These enzymes catalyse the hydrolysis of sphingomyelin, resulting in the formation of ceramide 1-phosphate and choline:
- sphingomyelin + H2O ceramide 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 3.1.4.4.[3] 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
References
- ↑ Carne, H.R.; Onon, Eleanor O. (19 January 1978). "Action of Corynebacterium ovis exotoxin on endothelial cells of blood vessels". Nature. 271 (5642): 246–248. doi:10.1038/271246a0. PMID 622164.
- ↑ Souček, Andrej; Michalec, Čestmír; Součková, Anna (13 January 1971). "Identification and characterization of a new enzyme of the group "phospholipase D" isolated from Corynebacterium ovis". Biochimica et Biophysica Acta. 227 (1): 116–128. doi:10.1016/0005-2744(71)90173-2. PMID 5543581.
- ↑ Murakami, M.T.; Gabdoulkhakov, A.; Fernandes-Pedrosa, M.F.; Tambourgi, D.V.; Arni, R.K. (2005). "Structural basis for metal ion coordination and the catalytic mechanism of sphingomyelinases D.". J.Biol.Chem. 280: 13658–13664. doi:10.1074/jbc.M412437200. PMID 15654080.
External links
- Sphingomyelin phosphodiesterase D at the US National Library of Medicine Medical Subject Headings (MeSH)
- http://www.arachnoserver.org/toxincard.html?id=138