Lipase-specific foldases

被引:185
作者
Rosenau, F
Tommassen, J
Jaeger, KE [1 ]
机构
[1] Univ Dusseldorf, Forschungszentrum Julich, Inst Mol Enzymtechnol, D-52428 Julich, Germany
[2] Univ Utrecht, Dept Mol Microbiol, NL-3584 CH Utrecht, Netherlands
[3] Univ Utrecht, Biomembrane Inst, NL-3584 CH Utrecht, Netherlands
关键词
chaperone proteins; foldases; protein engineering; protein folding; secretion;
D O I
10.1002/cbic.200300761
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Liposes represent the most important class of enzymes used in biotechnology. Many bacteria produce and secrete liposes but the enzymes originating from Pseudomonas and Burkholderia species seem to be particularly useful for a wide variety of different biocatalytic applications. These enzymes ore usually encoded in on 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 liposes into their enzymatically active conformation.
引用
收藏
页码:153 / 161
页数:9
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