A molecular model for interfacial activation in phospholipase A2.

J Warwicker

doi:10.1016/s0014-5793(97)00119-1

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A molecular model for interfacial activation in phospholipase A2.

J Warwicker

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Abstract

Electrostatic calculations predict that amino-terminal conformation and ionisation contribute significantly to transition state stability in phospholipase A2, so that control of these factors by binding to aggregated substrate provides a plausible mechanism for interfacial activation. In particular, it is suggested that a part of the pH dependence of interfacial activity may arise from transient deprotonation of an ordered amino-terminus. Interface charge and the detailed structure of the interfacial complex are also predicted to influence catalytic activity. The model is compared with available biochemical data.

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Animals Enzyme Activation Enzyme Stability Hydrogen-Ion Concentration Models, Molecular Pancreas Phospholipases A Phospholipases A2 Protein Conformation Protein Structure, Secondary Static Electricity Swine Thermodynamics Journal Article Research Support, Non-U.S. Gov't

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J Warwicker. 1997-03-10. A molecular model for interfacial activation in phospholipase A2.. https://doi.org/10.1016/s0014-5793(97)00119-1

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