Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases

被引：49

作者：

Cipolla, Alexandre

Delbrassine, Francois

Da Lage, Jean-Luc ^{[2
,3
]}

Feller, Georges ^{[1
]}

机构：

[1] Univ Liege, Ctr Prot Engn, Biochem Lab, Inst Chem B6A, B-4000 Liege, Belgium

[2] CNRS, Evolut Genomes & Speciat UPR9034, F-91198 Gif Sur Yvette, France

[3] Univ Paris 11, F-91405 Orsay, France

来源：

BIOCHIMIE | 2012年 / 94卷 / 09期

关键词：

Alpha-amylase; Extremophiles; Antarctic; Differential scanning calorimetry; Protein stability; COLD ADAPTATION; CONFORMATIONAL FLEXIBILITY; EVOLUTIONARY RELATIONSHIPS; STEPWISE ADAPTATIONS; STABILITY; PROTEINS; ENZYMES; SIMILARITIES; ACTIVATION; BACTERIA;

D O I：

10.1016/j.biochi.2012.05.013

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

The functional and structural adaptations to temperature have been addressed in homologous chloride-dependent alpha-amylases from a psychrophilic Antarctic bacterium, the ectothermic fruit fly, the homeothermic pig and from a thermophilic actinomycete. This series covers nearly all temperatures encountered by living organisms. We report a striking continuum in the functional properties of these enzymes coupled to their structural stability and related to the thermal regime of the source organism. In particular, thermal stability recorded by intrinsic fluorescence, circular dichroism and differential scanning calorimetry appears to be a compromise between the requirement for a stable native state and the proper structural dynamics to sustain the function at the environmental/physiological temperatures. The thermodependence of activity, the kinetic parameters, the activations parameters and fluorescence quenching support these activity-stability relationships in the investigated alpha-amylases. (C) 2012 Elsevier Masson SAS. All rights reserved.

引用

页码：1943 / 1950

页数：8

共 57 条

[1]

Structures of the psychrophilic Alteromonas haloplanctis α-amylase give insights into cold adaptation at a molecular level [J].