Premium
Lys‐49‐phospholipases A2 as active enzyme for β‐arachidonoyl phospholipid bilayer membranes
Author(s) -
Yamaguchi Yoko,
Shimohigashi Yasuyuki,
Chiwata Tsuyoshi,
Tani Ayako,
Chijiwa Takahisa,
Lomonte Bruno,
Ohno Motonori
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700203771
Subject(s) - myotoxin , chemistry , liposome , biochemistry , phosphatidylcholine , phospholipase a2 , enzyme , phospholipid , snake venom , vesicle , bilayer , lipid bilayer , arachidonic acid , membrane
Phospholipases A2 containing Lys‐49 have been reported to be extremely weak or inactive as enzyme. We have recently shown that basic proteins I and II (BP‐I and BP‐II), Lys‐49‐PLA2s isolated from the venom of Trimeresurus flavoviridis (Habu snake), are potent to hydrolyze the arachidonate of 2‐arachidonoyl‐1‐stearoyl‐L‐3‐phosphatidylcholine (ASPC) in bilayer vesicles. In order to ensure such enzymatic activity of Lys‐49‐PLA2s, two other Lys‐49‐PLA2s from different snake venoms, myotoxin II (from Bothrops asper) and App‐K49 (form Agkistrodon piscivorus piscivorus), were examined. Myotoxin II was found to be very active, even more potent than BP‐II, liberating about 80% of arachidonic acid from liposomes. App‐K49 was also active (about 50%) for ASPC liposomes. They were very weak or almost inactive for ASPC micelles and monomers. All these Lys‐49‐PLA2s were inactive for ASPC liposomes in the absence of Ca2+. These results clearly demonstrated that Lys‐49‐PLA2s are the enzymes to hydrolyze the C2‐ester bond of ASPC in bilayer membranes.