Xylanase from the psychrophilic yeast Cryptococcus adeliae

被引:94
作者
Petrescu, I
Lamotte-Brasseur, J
Chessa, JP
Ntarima, P
Claeyssens, M
Devreese, B
Marino, G
Gerday, C [1 ]
机构
[1] Univ Liege, Biochim Lab, Inst Chim B6, Liege, Belgium
[2] Eurogentec SA, Seraing, Belgium
[3] Univ Liege, Ctr Ingn Prot, Inst Chim B6, Liege, Belgium
[4] State Univ Ghent, Biochem Lab, B-9000 Ghent, Belgium
[5] Univ Naples Federico II, Dept Organ & Biol Chem, Naples, Italy
关键词
xylanases; psychrophile; yeast; molecular adaptation; molecular modeling;
D O I
10.1007/s007920070028
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
A xylanase belonging to family 10 is produced by Cryptococcus adeliae, an Antarctic yeast that exhibits optimal growth at low temperature, The mature glycosylated xylanase secreted by C. adeliae is composed of 338 amino acid residues and 26 +/- 3 osidic residues, and shares 84% identity with its mesophilic counterpart from C. albidus. The xylanase from C. adeliae is less thermostable than its mesophilic homologue when the residual activities are compared, and this difference was confirmed by differential scanning calorimetry experiments. In the range 0 degrees-20 degrees C, the cold-adapted xylanase displays a lower activation energy and a higher catalytic efficiency. All these observations suggest a less compact, more flexible molecular structure. Analysis of computerized molecular models built up for both psychrophilic and mesophilic xylanases indicates that the adaptation to cold consists of discrete changes in the tridimensional structure: of 53 substitutions, 22 are presumably involved in the adaptation process. These changes lead mainly to a less compact hydrophobic packing, to the loss of one salt bridge, and to a destabilization of the macrodipoles of the helices.
引用
收藏
页码:137 / 144
页数:8
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