Family I.3 lipase: bacterial lipases secreted by the type I secretion system

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.

Crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conformation

“…In fact, some family I.3 lipases contain only six RTX repeats [2]. Further deletion of the repeats or mutation abolishes the repeats' ability to form b-roll motif, and greatly decreases secretion efficiency, proteolysis stability, and enzymatic activity [9,10].…”

“…They are secreted via the type I secretion system (T1SS) [2]. T1SS consists of three subunit proteins, which form a channel that spans the inner and outer membranes of Gram-negative bacteria.…”

X-ray Crystallographic and MD Simulation Studies on the Mechanism of Interfacial Activation of a Family I.3 Lipase with Two Lids

“…Family I.3 lipase is a subfamily of Gram-negative bacterial true lipases and is secreted by a type I secretion system (T1SS). 2,3 It is produced by limited species of bacteria, with several Pseudomonas and Serratia species being the only producers reported so far. Like other proteins that are secreted by the T1SS, family I.3 lipase consists of two domains, an N-domain containing the lipase catalytic triad (Ser, His, Asp) and a C-domain containing repeats of the RTX (repeats in toxins) motif and a secretion signal near its C-terminus.…”

Characterization and optimization of lipase activity produced by Pseudomonas monteilli 2403-KY120354 isolated from ground beef

“…As shown in Figure 3, lipase activity was recorded as 14 U/mL at 20°C and it was gradually increased until it reaches 30 U/mL at 40°C that was the optimum temperature, and then decreased by increasing temperature. Angkawidjaja and Kanaya (2006) reported that in general, the optimum growth and enzymes activity of Pseudomonas genus were obtained in the mesophilic or thermophilic range of temperatures. According to Adan et al (2009), Pseudomonas spp.…”