Phospholipase

Phospholipase cleavage sites. An enzyme that displays both PLA1 and PLA2 activities is called a Phospholipase B.

A phospholipase is an enzyme that hydrolyzes phospholipids^[1] into fatty acids and other lipophilic substances. There are four major classes, termed A, B, C and D, which are distinguished by the type of reaction which they catalyze:

• Phospholipase A
  • Phospholipase A1 – cleaves the SN-1 acyl chain (where SN refers to stereospecific numbering).
  • Phospholipase A2 – cleaves the SN-2 acyl chain, releasing arachidonic acid.
• Phospholipase B – cleaves both SN-1 and SN-2 acyl chains; this enzyme is also known as a lysophospholipase.
• Phospholipase C – cleaves before the phosphate, releasing diacylglycerol and a phosphate-containing head group. Phospholipase Cs play a central role in signal transduction, releasing the second messenger inositol triphosphate.
• Phospholipase D – cleaves after the phosphate, releasing phosphatidic acid and an alcohol.

Types C and D are considered phosphodiesterases.

Endothelial lipase is primarily a phospholipase.^[2]

Phospholipase A2 acts on the intact lecithin molecule and hydrolyses the fatty acid esterified to the second carbon atom. The resulting products are lysolecithin and a fatty acid. Phospholipase A2 is an enzyme present in the venom of bees and viper snakes.^[3]

See also

• Patatin-like phospholipase
• Infantile neuroaxonal dystrophy

References

Further reading

• Tappia, Paramjit S. & Dhalla, Naranjan S. (Editors): Phospholipases in Health and Disease. Springer, 2014. ISBN 978-1-4939-0463-1 [Print]; ISBN 978-1-4939-0464-8 [eBook]

External links

• Phospholipases at the US National Library of Medicine Medical Subject Headings (MeSH)