Conference paper

Understanding Lipase Action and Selectivity

Peter Stadler ; Department of Biochemistry and Food Chemistry, Technische Universitat Graz, Spezialforschungsbereich Biokatalyse, Petersgasse 12/11, A-8010 Graz, Austria
Andrea Kovac ; Department of Biochemistry and Food Chemistry, Technische Universitat Graz, Spezialforschungsbereich Biokatalyse, Petersgasse 12/11, A-8010 Graz, Austria
Fritz Paltauf ; Department of Biochemistry and Food Chemistry, Technische Universitat Graz, Spezialforschungsbereich Biokatalyse, Petersgasse 12/11, A-8010 Graz, Austria

Abstract

In this article, a survey of recent lipase research, with special emphasis on molecular structure-function relationships, is presented. Determination 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 proteases is responsible for the cleavage of substrate ester bonds, involving the formation of an acyl-enzyme intermediate. Comparative structural studies revealed a common three dimensional fold and a superimposable topology of the catalytic machinery in lipases, esterases, and other hydrolytic enzymes. Availability of three dimensional structures is the basis for .understanding the mechanism of lipase catalysis and for elucidation of the molecular interactions that result in variant selectivities towards triacylglycerols and their analogs.

Keywords

Hrčak ID:

136724

URI

https://hrcak.srce.hr/136724

Publication date:

1.9.1995.

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