UNDERSTANDING LIPASE ACTION AND SELECTIVITY

In this article, a survey of recent lipase research, with special emph asis on molecular structure-function relationships, is presented. Dete rmination of crystallographic structures of lipases from microbial and mammalian origin has shed light on the molecular mechanism of lipase catalyzed acyl ester hydrolysis. A catalytic triad similar to serine p roteases is responsible for the cleavage of substrate ester bonds, inv olving the formation of an acyl-enzyme intermediate. Comparative struc tural studies revealed a common three dimensional fold and a superimpo sable topology of the catalytic machinery in lipases, esterases, and o ther hydrolytic enzymes. Availability of three dimensional structures is the basis for understanding the mechanism of lipase catalysis and f or elucidation of the molecular interactions that result in variant se lectivities towards triacylglycerols and their analogs.