ArticleBiophysical journal2013
A model for the interfacial kinetics of phospholipase D activity on long-chain lipids.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Lipid-associated oral delivery: Mechanisms and analysis of oral absorption enhancement.Journal of controlled release : official journal of the Controlled Release Society · 2016Review
- Polyvalent Catalysts Operating on Polyvalent Substrates: A Model for Surface-Controlled Reactivity.Angewandte Chemie (International ed. in English) · 2016Article
- Functional Characterization of the N-Terminal C2 Domain fromBioMed research international · 2016Article
- Surface dilution kinetics of phospholipase A(2) catalyzed lipid-bilayer hydrolysis.The journal of physical chemistry. B · 2014Article
- Monitoring phosphatidic acid formation in intact phosphatidylcholine bilayers upon phospholipase D catalysis.Analytical chemistry · 2014Article
- A new model of interfacial kinetics for phospholipases.Biophysical journal · 2013Article
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5 authors.
Funding
Abstract
The membrane-active enzyme phospholipase D (PLD) catalyzes the hydrolysis of the phosphodiester bond in phospholipids and plays a critical role in cell signaling. This catalytic reaction proceeds on lipid-water interfaces and is an example of heterogeneous catalysis in biology. Recently we showed that planar lipid bilayers, a previously unexplored model membrane for these kinetic studies, can be used for monitoring interfacial catalytic reactions under well-defined experimental conditions with chemical and electrical access to both sides of the lipid membrane. Employing an assay that relies on the conductance of the pore-forming peptide gramicidin A to monitor PLD activity, the work presented here reveals the kinetics of hydrolysis of long-chain phosphatidylcholine lipids in situ. We have developed an extension of a basic kinetic model for interfacial catalysis that includes product activation and substrate depletion. This model describes the kinetic behavior very well and reveals two kinetic parameters, the specificity constant and the interfacial quality constant. This approach results in a simple and general model to account for product accumulation in interfacial enzyme kinetics.
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