Psychrophilic enzymes: a thermodynamic challenge

被引:240
作者
Gerday, C
Aittaleb, M
Arpigny, JL
Baise, E
Chessa, JP
Garsoux, G
Petrescu, I
Feller, G
机构
[1] Laboratory of Biochemistry, Inst. Chem., B6 Univ. Liege, Sart-T.
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1997年 / 1342卷 / 02期
关键词
psychrophile; adaptation to cold; Antarctic microorganism;
D O I
10.1016/S0167-4838(97)00093-9
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
Psychrophilic microorganisms, hosts of permanently cold habitats, produce enzymes which are adapted to work at low temperatures. When compared to their mesophilic counterparts, these enzymes display a higher catalytic efficiency over a temperature range of roughly 0-30 degrees C and a high thermosensitivity. The molecular characteristics of cold enzymes originating from Antarctic bacteria have been approached through protein modelling and X-ray crystallography. The deduced three-dimensional structures of cold alpha-amylase, beta-lactamase, lipase and subtilisin have been compared to their mesophilic homologs. It appears that the molecular adaptation resides in a weakening of the intramolecular interactions, and in some cases in an increase of the interaction with the solvent, leading to more flexible molecular edifices capable of performing catalysis at a lower energy cost. (C) 1997 Elsevier Science B.V.
引用
收藏
页码:119 / 131
页数:13
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