Stability and structural analysis of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23.

@article{Feller1994StabilityAS,
  title={Stability and structural analysis of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23.},
  author={Georges Feller and Françoise Payan and F Theys and Minxie Qian and Richard Haser and Charles Gerday},
  journal={European journal of biochemistry},
  year={1994},
  volume={222 2},
  pages={441-7}
}
The alpha-amylase secreted by the antarctic bacterium Alteromonas haloplanctis displays 66% amino acid sequence similarity with porcine pancreatic alpha-amylase. The psychrophilic alpha-amylase is however characterized by a sevenfold higher kcat and kcat/Km values at 4 degrees C and a lower conformational stability estimated as 10 kJ.mol-1 with respect to the porcine enzyme. It is proposed that both properties arise from an increase in molecular flexibility required to compensate for the… CONTINUE READING