Modified lipoprotein lipase catalyzes ester synthesis in benzene. Substrate specificity.
Modified lipoprotein lipase catalyzed the synthesis of trilaurin from mono- or diacylglycerol and fatty acid and also the synthesis of ester from fatty acid and alcohol in benzene. In the ester synthesis reaction, the longer the chain length of fatty acid or alcohol, the higher the ester synthesis activity. The ester synthesis was competitively inhibited by fatty acids with branch of carbon chain at the position neighboring the carboxyl group. Other substrates including secondary and tertiary alcohols and carboxylic acids having benzene ring were tested and discussed in relation to the ester synthesis.
D001554:Benzene; D004075:Diglycerides / Q000378:metabolism; D004951:Esterification; D005227:Fatty Acids / Q000378:metabolism; D005989:Glycerides / Q000378:metabolism; D007700:Kinetics; D007850:Lauric Acids / Q000378:metabolism; D008071:Lipoprotein Lipase / Q000494:pharmacology*; D011092:Polyethylene Glycols / Q000494:pharmacology*; D013379:Substrate Specificity; D014280:Triglycerides / Q000138:chemical synthesis*
D004075:Diglycerides; D005227:Fatty Acids; D005989:Glycerides; D007850:Lauric Acids; D014280:Triglycerides; C030358:lauric acid; D011092:Polyethylene Glycols; C029761:2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine; C004565:trilaurin; D008071:Lipoprotein Lipase; D001554:Benzene