6533b86dfe1ef96bd12ca06d

RESEARCH PRODUCT

Activation of bee venom phospholipase A2 through a peptide-enzyme complex

Jon R. AppelIsmael MingarroEnrique Pérez-payáRichard A. HoughtenSylvie E. BlondelleClemencia Pinilla

subject

Enzyme complexProtein ConformationMolecular Sequence DataBiophysicsPhospholipidPeptidePhospholipaseBiochemistrycomplex mixturesAbellesMelittinAntibodiesPhospholipases AProtein Structure Secondarychemistry.chemical_compoundEnzyme activatorPhospholipase A2Structural BiologyGeneticsAnimalsAmino Acid SequencePhospholipaseMolecular BiologyPeptide sequencePeptide-enzyme complexchemistry.chemical_classificationbiologyCircular DichroismMembrane ProteinsMelittinCell BiologyMelittenEnzyme ActivationBee VenomsPhospholipases A2chemistryBiochemistryLiposomesbiology.proteinPèptidsPeptides

description

AbstractPhospholipase 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 (α-helix, β-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.

yearjournalcountryeditionlanguage
1995-09-18
10.1016/0014-5793(95)00964-bhttps://doi.org/10.1016/0014-5793(95)00964-B