A chemical description of the action of phospholipase A2 (PLA2) can now be inferred with confidence from three high-resolution x-ray crystal structures. The first is the structure of the PLA2 from the venom of the Chinese cobra (Naja naja atra) in a complex with a phosphonate transition-state analogue. This enzyme is typical of a large, well-studied homologous family of PLA2S. The second is a similar complex with the evolutionarily distant bee-venom PLA2. The third structure is the uninhibited PLA2 from Chinese cobra venom. Despite the different molecular architectures of the cobra and bee-venom PLA2s, the transition-state analogue interacts in a nearly identical way with the catalytic machinery of both enzymes. The disposition of the fatty-acid side chains suggests a common access route of the substrate from its position in the lipid aggregate to its productive interaction with the active site. Comparison of the cobra-venom complex with the uninhibited enzyme indicates that optimal binding and catalysis at the lipid-water interface is due to facilitated substrate diffusion from the interfacial binding surface to the catalytic site rather than an allosteric change in the enzyme9s structure. However, a second bound calcium ion changes its position upon the binding of the transition-state analogue, suggesting a mechanism for augmenting the critical electrophile.

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Interfacial catalysis: the mechanism of phospholipase A2

Structure and function of phospholiphase A2

Methods for lipase detection and assay: a critical review

This review focuses on the use of immobilized lipase technology to effect hydrolysis, ester synthesis, and interesterification reactions. The various immobilization procedures, reactor configurations, and process considerations are all reviewed and discussed.

P Desnuelle

Papers

Further studies of mode of action of lipolytic enzymes.

Effects of colipase on hydrolysis of monomolecular films by lipase.