Gr. Grotendorst et Da. Hessinger, Enzymatic characterization of the major phospholipase A(2) component of sea anemone (Aiptasia pallida) nematocyst venom, TOXICON, 38(7), 2000, pp. 931-943
The purified beta phospholipase A(2) (PLA(2); EC 3.1.1.4) (PLA(2)) from sea
anemone (Aiptasia pallida) nematocysts is larger and more labile than othe
r known venom PLA(2)s. In common with all other known venoms and most secre
tory PLA(2)s, the beta PLA(2) requires mM Ca2+ for optimal activity and is
surface-activated by aggregated lipids such as mixed micelles of detergent
and phospholipid. The beta PLA(2) exhibits an unusually steep and narrow pH
optimum of activity at pH 7.7. The effects of changes in pH on the activit
y of the enzyme suggest that the active site contains functional groups hav
ing a pK's of about 7.0 and 8.0, The effects of temperature on beta PLA(2)
activity show a marked decrease in the energy of activation above the pre-t
ransition temperature, suggesting that the enzyme "melts" both fatty chains
in order for catalysis to occur. (C) 2000 Elsevier Science Ltd. All rights
reserved.