Phospholipase A2 is an enzyme that hydrolyzes glycerophospholipids, cleaving free fatty acids from the second carbon on the glycerol molecule. Phospholipase is the main contributor to the neurotoxicity of snake venoms, such as coralsnake venom.  In its native form, the phospholipase A2 holoenzyme contains calcium as the divalent metal ion cofactor. In this study, the endogenous calcium ion was removed and other divalent metals were tested as possible replacements for calcium. Various metals were tested for their ability to function as a replacement cofactor to activate the enzyme and for their binding affinity in comparison to calcium. The chelating agent EDTA was used to sequester the calcium from phospholipase A2, allowing their replacement with other divalent metals.  The results of the study will reveal whether metals other than calcium can active the enzyme, and through binding competition studies indicate the relative binding affinity of the enzyme for various metal ions.

Metal ion cofactor requirements for phospholipase A2

245th National Meeting (2013)

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