Molecular adaptations to cold in psychrophilic enzymes

被引:181
|
作者
Feller, G [1 ]
机构
[1] Univ Liege, Inst Chem B6, Biochem Lab, B-4000 Liege, Belgium
关键词
psychrophile; extremophile; enzyme kinetics; crystal structure; folding; mutagenesis; biophysics;
D O I
10.1007/s00018-003-2155-3
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
Psychrophiles or cold-loving organisms successfully colonize cold environments of the Earth's biosphere. To cope with the reduction of chemical reaction rates induced by low temperatures, these organisms synthesize enzymes characterized by a high catalytic activity at low temperatures associated, however, with low thermal stability. Thanks to recent advances provided by Xray crystallography, protein engineering and biophysical studies, we are beginning to understand the molecular adaptations responsible for these properties which appear to be relatively diverse. The emerging picture suggests that psychrophilic enzymes utilize an improved flexibility of the structures involved in the catalytic cycle, whereas other protein regions if not implicated in catalysis may or may not be subjected to genetic drift.
引用
收藏
页码:648 / 662
页数:15
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