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Defining Substrate Specificities for Lipase and Phospholipase Candidates

Defining Substrate Specificities for Lipase and Phospholipase Candidates

Published on: November 23, 2016

Substrate specificity of lysophospholipase D which produces bioactive lysophosphatidic acids in rat plasma.

A Tokumura¹, Y Nishioka, O Yoshimoto

¹Faculty of Pharmaceutical Sciences, The University of Tokushima, Tokushima, 1-78, Shomachi 770-8505, Japan. tokumura@ph.tokushima-u.ac.jp

Biochimica Et Biophysica Acta

|March 5, 1999

Summary

Lysophospholipase D in rat plasma preferentially hydrolyzes unsaturated lysophosphatidylcholines (LPCs). Protein association does not dictate this preference, suggesting free unsaturated LPCs are preferred substrates.

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Area of Science:

Biochemistry
Enzymology
Lipid Metabolism

Background:

Lysophospholipase D (lysoPLD) in rat plasma hydrolyzes lysophosphatidylcholines (LPCs) to lysophosphatidic acids.
Previous work indicated a preference for unsaturated LPCs over saturated LPCs.

Purpose of the Study:

To investigate if LPC association with plasma proteins affects lysoPLD's substrate preference.
To determine the role of protein binding in lysoPLD's specificity for unsaturated LPCs.

Main Methods:

Analysis of LPC distribution in rat plasma protein fractions (albumin, lipoproteins).
Incubation of rat plasma with LPCs at 37°C and measurement of hydrolysis products.
Experiments using Nagase analbuminemic rats to assess the role of albumin-LPC complexes.
Characterization of LPC isomer forms (1-acyl) in rat plasma.

Main Results:

LPCs were predominantly found in the lipoprotein-poor fraction and associated with albumin.
LPC distribution among protein fractions did not correlate with lysoPLD hydrolysis rates.
Albumin-LPC complexes were not essential; lipoprotein-associated LPCs were good substrates.
Both saturated and unsaturated LPCs exist mainly as 1-acyl isomers, ruling out positional isomerism as the basis for preference.
LysoPLD showed higher affinity for free unsaturated LPCs (equilibrated with protein-bound forms) than for saturated LPCs or PAF analogs.

Conclusions:

The substrate specificity of rat plasma lysophospholipase D for unsaturated lysophosphatidylcholines is not determined by their distribution among plasma protein fractions.
The enzyme exhibits a higher affinity for free unsaturated acyl-type LPCs, irrespective of their equilibration with albumin or lipoproteins, compared to saturated forms.