Enzymatic characterization of the major phospholipase A2 component of sea anemone (Aiptasia pallida) nematocyst venom

Gary R. Grotendorst; David A. Hessinger

doi:10.1016/S0041-0101(99)00206-8

Enzymatic characterization of the major phospholipase A₂ component of sea anemone (Aiptasia pallida) nematocyst venom

Gary R. Grotendorst, David A. Hessinger

Physiology Division

Research output: Contribution to journal › Article › peer-review

Abstract

The purified β phospholipase A₂ (PLA₂; EC 3.1.1.4) (PLA₂) from sea anemone (Aiptasia pallida) nematocysts is larger and more labile than other known venom PLA₂s. In common with all other known venoms and most secretory PLA₂s, the β PLA₂ requires mM Ca²⁺ for optimal activity and is surface- activated by aggregated lipids such as mixed micelles of detergent and phospholipid. The β PLA₂ exhibits an unusually steep and narrow pH optimum of activity at pH 7.7. The effects of changes in pH on the activity of the enzyme suggest that the active site contains functional groups having a pKs of about 7.0 and 8.0. The effects of temperature on β PLA₂ activity show a marked decrease in the energy of activation above the pre-transition temperature, suggesting that the enzyme 'melts' both fatty chains in order for catalysis to occur. (C) 2000 Elsevier Science Ltd.

Original language	English
Pages (from-to)	931-943
Number of pages	13
Journal	Toxicon
Volume	38
Issue number	7
DOIs	https://doi.org/10.1016/S0041-0101(99)00206-8
State	Published - Jul 2000

ASJC Scopus Subject Areas

Toxicology

Keywords

Aiptasia pallida
Hemolysis
Nematocyst
Phospholipase A
Sea anemone
Toxin

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title = "Enzymatic characterization of the major phospholipase A2 component of sea anemone (Aiptasia pallida) nematocyst venom",

abstract = "The purified β phospholipase A2 (PLA2; EC 3.1.1.4) (PLA2) from sea anemone (Aiptasia pallida) nematocysts is larger and more labile than other known venom PLA2s. In common with all other known venoms and most secretory PLA2s, the β PLA2 requires mM Ca2+ for optimal activity and is surface- activated by aggregated lipids such as mixed micelles of detergent and phospholipid. The β PLA2 exhibits an unusually steep and narrow pH optimum of activity at pH 7.7. The effects of changes in pH on the activity of the enzyme suggest that the active site contains functional groups having a pKs of about 7.0 and 8.0. The effects of temperature on β PLA2 activity show a marked decrease in the energy of activation above the pre-transition temperature, suggesting that the enzyme 'melts' both fatty chains in order for catalysis to occur. (C) 2000 Elsevier Science Ltd.",

keywords = "Aiptasia pallida, Hemolysis, Nematocyst, Phospholipase A, Sea anemone, Toxin",

author = "Grotendorst, {Gary R.} and Hessinger, {David A.}",

note = "Funding Information: This research was supported by NIEHS Grant ESO 2182-03 and by the Florida Sea Grant Program of NOAA to D.A.H.",

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AU - Hessinger, David A.

N1 - Funding Information: This research was supported by NIEHS Grant ESO 2182-03 and by the Florida Sea Grant Program of NOAA to D.A.H.

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N2 - The purified β phospholipase A2 (PLA2; EC 3.1.1.4) (PLA2) from sea anemone (Aiptasia pallida) nematocysts is larger and more labile than other known venom PLA2s. In common with all other known venoms and most secretory PLA2s, the β PLA2 requires mM Ca2+ for optimal activity and is surface- activated by aggregated lipids such as mixed micelles of detergent and phospholipid. The β PLA2 exhibits an unusually steep and narrow pH optimum of activity at pH 7.7. The effects of changes in pH on the activity of the enzyme suggest that the active site contains functional groups having a pKs of about 7.0 and 8.0. The effects of temperature on β PLA2 activity show a marked decrease in the energy of activation above the pre-transition temperature, suggesting that the enzyme 'melts' both fatty chains in order for catalysis to occur. (C) 2000 Elsevier Science Ltd.

AB - The purified β phospholipase A2 (PLA2; EC 3.1.1.4) (PLA2) from sea anemone (Aiptasia pallida) nematocysts is larger and more labile than other known venom PLA2s. In common with all other known venoms and most secretory PLA2s, the β PLA2 requires mM Ca2+ for optimal activity and is surface- activated by aggregated lipids such as mixed micelles of detergent and phospholipid. The β PLA2 exhibits an unusually steep and narrow pH optimum of activity at pH 7.7. The effects of changes in pH on the activity of the enzyme suggest that the active site contains functional groups having a pKs of about 7.0 and 8.0. The effects of temperature on β PLA2 activity show a marked decrease in the energy of activation above the pre-transition temperature, suggesting that the enzyme 'melts' both fatty chains in order for catalysis to occur. (C) 2000 Elsevier Science Ltd.

KW - Aiptasia pallida

KW - Hemolysis

KW - Nematocyst

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KW - Sea anemone

KW - Toxin

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