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Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
The substrate specificity of glycerol ester hydrolase from pig aorta and serum
1Department of General Chemistry, Medical Academy, Poznań, Poland.
Abstract:
The activity of glycerol ester hydrolase (GEH) from aorta wall, at optimum pH and triacylglycerol substrate concentration (optimal for each substrate) decreased in the following order: C18:1 greater than or equal to C18:2 greater than or equal to C18:0 greater than or equal to C18:3 greater than or equal to C16:0. At optimum pH and the same substrate concentration (1 mM), the activity of GEH from aorta wall decreased in a slightly different order: C18:1 greater than or equal to C18:2 greater than or equal to C18:3 greater than C18:0 greater than C16:0 and that of the enzyme from serum in the order: C18:1 = C18:3 greater than C18:2 greater than or equal to C16:0 greater than or equal to C18:0. These differences in substrate affinity of GEH may influence the metabolism and accumulation of acylalcohols and alcohols in arterial wall and serum.
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