Lipase-specific foldases.
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.
Rosenau
Frank
F
Institut für Molekulare Enzymtechnologie, Heinrich-Heine-Universität Düsseldorf, Forschungszentrum Jülich, 52428 Jülich, Germany.
Tommassen
Jan
J
Jaeger
Karl-Erich
KE
D000595:Amino Acid Sequence; D015964:Gene Expression Regulation, Bacterial; D006090:Gram-Negative Bacteria / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D015850:Interleukin-6; D053605:Leukemia Inhibitory Factor; D008969:Molecular Sequence Data; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013379:Substrate Specificity
D015850:Interleukin-6; D053605:Leukemia Inhibitory Factor; D011506:Proteins