Abstract
Lipases play an important role in lipid metabolism and are produced by a variety of species. All lipases are members of the a/â hydrolase fold super-family. Also, lipases share a conserved active site signature, the Gly-Xaa-Ser-Xaa-Gly motif. To obtain an overview of this industrially and very important class of enzymes and their characteristics, we collected and classified bacterial lipases sequences available from protein databases. Here we proposed an updated and revised classification of family I bacterial true lipases based mainly on a comparison of their amino acid sequences and some fundamental physicochemical and biological properties. The result of this work has identified 11 subfamilies of “true” lipases. This work will therefore contribute to a faster identification and to an easier characterization and classification of novel bacterial lipolytic enzymes. Key words : Lipases, phylogenetic analysis, lipolytic enzymes.
Highlights
Lipases are glycerol ester hydrolases that act on acylglycerols to liberate fatty acids and glycerol
53 sequences of bacterial lipases belonging to the family I known as true lipases, are compared and classified according to conserved sequence motifs and same biological and physico-chemical properties of these enzymes
Representative lipase sequences were collected from the ExPASy and the National Center for Biotechnology Information (NCBI) server
Summary
Lipases are glycerol ester hydrolases that act on acylglycerols to liberate fatty acids and glycerol. There is an increasing interest in bacterial lipases because they represent the most versatile and widely used enzymes in biotechnological applications and organic chemistry (Reetz and Jaeger 1998). Lipases belong to many different protein families they have the same architecture, the α/β hydrolase fold as defined by Ollis et al (1992). Their activities rely mainly on a catalytic triad usually formed by Ser, His and Asp residues (Arpigny and Jaeger, 1999). 53 sequences of bacterial lipases belonging to the family I known as true lipases, are compared and classified according to conserved sequence motifs and same biological and physico-chemical properties of these enzymes.
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