Rosenau_2004_Chembiochem_5_152

Reference

Title : Lipase-specific foldases - Rosenau_2004_Chembiochem_5_152
Author(s) : Rosenau F , Tommassen J , Jaeger KE
Ref : Chembiochem , 5 :152 , 2004
Abstract :

Lipases represent the most important class of enzymes used in biotechnology. Many bacteria produce and secrete lipases but the enzymes originating from Pseudomonas and Burkholderia species seem to be particularly useful for a wide variety of different biocatalytic applications. These enzymes are usually encoded in an operon together with a second gene which codes for a lipase-specific foldase, Lif, which is necessary to obtain enzymatically active lipase. A detailed analysis based on amino acid homology has suggested the classification of Lif proteins into four different families and also revealed the presence of a conserved motif, Rx1x2FDY(F/C)L(S/T)A. Recent experimental evidence suggests that Lifs are so-called steric chaperones, which exert their physiological function by lowering energetic barriers during the folding of their cognate lipases, thereby providing essential steric information needed to fold lipases into their enzymatically active conformation.

PubMedSearch : Rosenau_2004_Chembiochem_5_152
PubMedID: 14760735

Related information

Citations formats

Rosenau F, Tommassen J, Jaeger KE (2004)
Lipase-specific foldases
Chembiochem 5 :152

Rosenau F, Tommassen J, Jaeger KE (2004)
Chembiochem 5 :152