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Literature summary for 3.1.1.4 extracted from

  • Jackman, J.A.; Cho, N.J.; Duran, R.S.; Frank, C.W.
    Interfacial binding dynamics of bee venom phospholipase A2 investigated by dynamic light scattering and quartz crystal microbalance (2010), Langmuir, 26, 4103-4112.
    View publication on PubMed
Search for more literature for 3.1.1.4

Application

Application Comment Organism
drug development new pharmaceutical approaches against PLA2 activity can be designed to prevent either membrane adsorption or nonhydrolytic bilayer-disrupting activity, both of which are necessary for enzymatic activity, opening up a new set of specific functional targets for inhibitor design Apis mellifera

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ free Ca2+ is required for interaction between PLA2 and vesicles under catalytic conditions, Ca2+ addition for activation of PLA2 under initially noncatalytic conditions. Differences between enzymatic activity under initially catalytic and noncatalytic conditions, membrane binding under noncatalytic conditions must either cause PLA2 to adopt a less favorable conformation for enzymatic activity or prevent a Ca2+ ion (after Ca2+ addition) from entering the active site pocket Apis mellifera

Organism

Organism UniProt Comment Textmining
Apis mellifera
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Source Tissue

Source Tissue Comment Organism Textmining
venom
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 Apis mellifera
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Storage Stability

Storage Stability Organism
4°C, 10 mM Tris buffer, pH 7.7, 150 mM NaCl, 2 mM EDTA Apis mellifera

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PLA2 shows low enzymatic activity toward positively charged vesicles due to a long lag period. PLA2 demonstrates a high degree of enzymatic activity toward negatively charged 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine and 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine/1,2-dioleoyl-sn-glycero-3-phosphatidylserine vesicles. Vesicle size distribution of zwitterionic 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine changes faster than that of 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine/1,2-dioleoyl-sn-glycero-3-phosphatidylserine 90:10 Apis mellifera ?
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Synonyms

Synonyms Comment Organism
secretory phospholipase A2
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 Apis mellifera
sPLA2
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 Apis mellifera

General Information

General Information Comment Organism
physiological function adsorption of PLA2 to model membranes is not primarily driven by electrostatic interactions. Subsequent lipid desorption, which is linked to the bilayer-disrupting activity of PLA2, is significantly affected by membrane electrostatics. Specifically, a nonhydrolytic bilayer-disrupting activity of PLA2 targets anionic membranes, triggering a change in bilayer topology Apis mellifera