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Sphingomyelin phosphodiesterase D

Class of enzymes

Summary

Class of enzymes

FieldValue
NameSphingomyelin phosphodiesterase D
EC_number3.1.4.41
CAS_number54992-31-3
captionCrystal structure of Sphingomyelin phosphodiesterase D, class II phospholipase D from the recluse spider Loxosceles intermedia (from PDB entry )

Sphingomyelin phosphodiesterase D (EC 3.1.4.41, sphingomyelinase D) is an enzyme of the sphingomyelin phosphodiesterase family with systematic name sphingomyelin ceramide-phosphohydrolase. These enzymes catalyse the hydrolysis of sphingomyelin, resulting in the formation of ceramide 1-phosphate and choline: : sphingomyelin + H2O \rightleftharpoons 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 . Sphingomyelinases D are produced by some spiders in their venoms, specifically the brown recluse (Loxosceles reclusa), 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.

References

References

  1. (June 2011). "Structure of a novel class II phospholipase D: catalytic cleft is modified by a disulphide bridge". Biochemical and Biophysical Research Communications.
  2. (January 1978). "Action of ''Corynebacterium ovis'' exotoxin on endothelial cells of blood vessels". Nature.
  3. (January 1971). "Identification and characterization of a new enzyme of the group "phospholipase D" isolated from Corynebacterium ovis". Biochimica et Biophysica Acta (BBA) - Enzymology.
  4. (April 2005). "Structural basis for metal ion coordination and the catalytic mechanism of sphingomyelinases D". The Journal of Biological Chemistry.
  5. (2015). "The Brown Recluse Spider". Cornell University Press.
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