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脂肪酶特异性折叠酶。

Lipase-specific foldases.

作者信息

Rosenau Frank, Tommassen Jan, Jaeger Karl-Erich

机构信息

Institut für Molekulare Enzymtechnologie, Heinrich-Heine-Universität Düsseldorf, Forschungszentrum Jülich, 52428 Jülich, Germany.

出版信息

Chembiochem. 2004 Feb 6;5(2):152-61. doi: 10.1002/cbic.200300761.

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.

摘要

脂肪酶是生物技术中使用的最重要的一类酶。许多细菌产生并分泌脂肪酶,但源自假单胞菌属和伯克霍尔德菌属的酶似乎对多种不同的生物催化应用特别有用。这些酶通常与第二个基因一起编码在一个操纵子中,该第二个基因编码一种脂肪酶特异性折叠酶Lif,它是获得具有酶活性的脂肪酶所必需的。基于氨基酸同源性的详细分析表明,Lif蛋白可分为四个不同的家族,还揭示了一个保守基序Rx1x2FDY(F/C)L(S/T)A的存在。最近的实验证据表明,Lif是所谓的空间伴侣,它们通过降低其同源脂肪酶折叠过程中的能量屏障来发挥其生理功能,从而提供将脂肪酶折叠成其酶活性构象所需的基本空间信息。

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