Substrate specificity of Staphylococcus aureus (TEN5) lipases with isomeric oleoyl- sn-glycerol ethers as substrates

• Published in: Chemistry and physics of lipids Vol. 47; no. 2; pp. 117 - 122
• Main Authors: Kötting, J., Eibl, H., Fehrenbach, F.-J.
• Format: Journal Article
• Language: English
• Published: Shannon Elsevier Ireland Ltd 01.06.1988; Elsevier Science
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Enzymes and enzyme inhibitors; ether lipids; Fundamental and applied biological sciences. Psychology; Glyceryl Ethers - metabolism; Hydrolases; Kinetics; Lipase - metabolism; lipases; Staphylococcus aureus; Staphylococcus aureus - enzymology; Stereoisomerism; stereospecificity; Substrate Specificity; stereospecificity; lipases; Staphylococcus aureus; ether lipids; Enzyme; Substrate specificity; Triacylglycerol lipase; Bacteria; Micrococcales; Stereospecificity; Micrococcaceae
• ISSN: 0009-3084; 1873-2941
• DOI: 10.1016/0009-3084(88)90080-1

For the first time fully protected substrates with only one hydrolizable ester bond have been used to analyze the substrate specificity of microbial lipases. In these substrates the ester is attached to the glycerol molecule in a precisely defined position. The use of three different substituents generates chirality and thus allows the analysis of positional specificities of individual lipases. Therefore, these new substrates have been used to study the enzymatic activities of two closely related lipases isolated from Staphylococcus aureus (TEN5) designated the 44 and 43 kDa lipase. The lipases, especially the 44 kDa molecule, show a high specificity for the hydrolysis of the ester in the sn-1 position ( S-configuration), which is hydrolyzed by a factor of ten faster than that in the sn-3 position. In addition, the study demonstrates for the first time that the rate of hydrolysis of a fatty acid ester attached to the sn-2 position of glycerol by microbial lipases depends on the configuration of the substrate molecule.