Sphingomyelin phosphodiesterase D explained
Sphingomyelin phosphodiesterase D |
Ec Number: | 3.1.4.41 |
Cas Number: | 54992-31-3 |
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 .
[3] Sphingomyelinases D are produced by some
spiders in their
venoms, specifically the
brown recluse (Loxosceles reclusa),
[4] 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 brown recluse spider bites.
See also
External links
- http://www.arachnoserver.org/toxincard.html?id=138
Notes and References
- Carne HR, Onon EO . Action of Corynebacterium ovis exotoxin on endothelial cells of blood vessels . Nature . 271 . 5642 . 246–8 . January 1978 . 622164 . 10.1038/271246a0 . 1978Natur.271..246C .
- Soucek A, Michalec C, Soucková A . Identification and characterization of a new enzyme of the group "phospholipase D" isolated from Corynebacterium ovis . Biochimica et Biophysica Acta (BBA) - Enzymology . 227 . 1 . 116–28 . January 1971 . 5543581 . 10.1016/0005-2744(71)90173-2 .
- Murakami MT, Fernandes-Pedrosa MF, Tambourgi DV, Arni RK . Structural basis for metal ion coordination and the catalytic mechanism of sphingomyelinases D . The Journal of Biological Chemistry . 280 . 14 . 13658–64 . April 2005 . 15654080 . 10.1074/jbc.M412437200 . free .
- Book: Vetter . Richard S. . The Brown Recluse Spider . 2015 . Cornell University Press . Ithaca, New York . 978-0-8014-7985-4 . 58 . 1st . 1 January 2020.