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Family I.3 lipase: bacterial lipases secreted by the type I secretion system
Authors:C Angkawidjaja  S Kanaya
Institution:(1) Laboratory of Molecular Biotechnology, Department of Material and Life Science, Division of Advanced Science and Biotechnology, Graduate School of Engineering, Osaka University, 2-1 Yamadaoka, Suita, Osaka 565-0871, Japan
Abstract:Based on the classification of bacterial lipolytic enzymes, family I.3 lipase is a member of the large group of Gram-negative bacterial true lipases. This lipase family is distinguished from other families not only by the amino acid sequence, but also by the secretion mechanism. Lipases of family I.3 are secreted via the well-known type I secretion system. Like most of proteins secreted via this system, family I.3 lipases are composed of two domains with distinct yet related functions. Recent years have seen an increasing amount of research on this lipase family, in terms of isolation, secretion mechanism, as well as biochemical and biophysical studies. This review describes our current knowledge on the structure-function relationships of family I.3 lipase, with an emphasis on its secretion mechanism. Received 18 April 2006; received after revision 3 July 2006; accepted 24 August 2006
Keywords:Family I  3 lipase  type I secretion system  β  -roll  Ca2+ binding                    Pseudomonas                  secretion signal  protein folding
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