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. 1977 May;74(5):1950–1954. doi: 10.1073/pnas.74.5.1950

Dual role of interfacial phospholipid in phospholipase A2 catalysis.

M F Roberts, R A Deems, E A Dennis
PMCID: PMC431050  PMID: 266715

Abstract

The results of crosslinking experiments with dimethyl suberimidate and gel filtration binding studies are used to delineate a detailed model for phospholipase A2(phosphatide 2-acyl-hydrolase, EC 3.1.1.4) action in the presence of Ca2+ on mixed micelles of Triton X-100 and phospholipid. Important features of the "dual-phospholipid" model are: (i) the use of the nonionic surfactant as an inert matrix that may influence lipid conformation but does not interact with the enzyme; (ii) the involvement of two lipid molecules in a single cycle of catalysis as an explanation for the "surface dilution" phenomenon; (iii) the requirement of an ordered reaction whereby divalent metal ion binds prior to phospholipid binding; and (iv) the induction by lipid substrate of an asymmetric dimer structure for the enzyme.

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1950

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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