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Lipase‐Specific Foldases
Author(s) -
Rosenau Frank,
Tommassen Jan,
Jaeger KarlErich
Publication year - 2004
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200300761
Subject(s) - foldase , lipase , biochemistry , enzyme , operon , biology , steric effects , thermostability , chemistry , gene , stereochemistry , escherichia coli , groel
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, Rx 1 x 2 FDY(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.