Wang C S, Hartsuck J A, Downs D
Lipoprotein and Atherosclerosis Research Program, Oklahoma Medical Research Foundation, Oklahoma City 73104.
Biochemistry. 1988 Jun 28;27(13):4834-40. doi: 10.1021/bi00413a038.
The simplest reaction scheme for the conversion of trioleoylglycerol to glycerol catalyzed by human milk bile salt activated lipase can be described by consecutive first-order reactions: triacylglycerol k1----diacylglycerol k2----monoacylglycerol k3----glycerol. In these equations, k1, k2, and k3 represent the pseudo-first-order rate constants for the indicated reactions. The results from this study show that although the relative ratio of k2/k1 or k3/k1 may change somewhat, depending on the reaction conditions, the enzyme has a reactivity with the order of dioleoylglycerol greater than trioleoylglycerol greater than monooleoylglycerol. The incomplete equilibration of the intermediary diacylglycerol and monoacylglycerol with the bulk of the substrate during sequential lipolysis of triacylglycerol provides a means for their efficient lipolysis and minimizes the effect of partial acylglycerol as competitive substrates for intact triacylglycerol lipolysis. Taurocholate functions both as an activator of the enzyme and also as fatty acid acceptor to relieve product inhibition. In the presence of sufficient taurocholate, bovine serum albumin is no longer required as a fatty acid acceptor for the in vitro lipolysis.
