Activation of bee venom phospholipase A2 through a peptide-enzyme complex.
Phospholipase A2 activation by membrane-bound peptides was investigated in order to understand the role of the membrane-induced conformation on activation, and to examine the occurrence of a peptide-enzyme complex at the lipid/water interface. For the peptides studies, bee venom phospholipase A2 was stimulated regardless of the membrane-bound conformation (alpha-helix, beta-sheet or random coil). Using antisera raised against melittin, we were able to demonstrate the occurrence of a calcium-dependent complex involving the enzyme, phospholipid substrate, and peptide.
Mingarro
I
I
Torrey Pines Institute for Molecular Studies, San Diego, CA 92121, USA.
Pérez-Payá
E
E
Pinilla
C
C
Appel
J R
JR
Houghten
R A
RA
Blondelle
S E
SE
D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000276:immunology; D001514:Bee Venoms / Q000201:enzymology*; D002942:Circular Dichroism; D004789:Enzyme Activation; D008081:Liposomes / Q000378:metabolism; D008555:Melitten / Q000276:immunology / Q000494:pharmacology*; D008565:Membrane Proteins / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D010741:Phospholipases A / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D054467:Phospholipases A2; D011487:Protein Conformation; D017433:Protein Structure, Secondary
D000906:Antibodies; D001514:Bee Venoms; D008081:Liposomes; D008565:Membrane Proteins; D010455:Peptides; D008555:Melitten; D010741:Phospholipases A; D054467:Phospholipases A2