Purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23.

@article{Feller1992PurificationCA,
  title={Purification, characterization, and nucleotide sequence of the thermolabile alpha-amylase from the antarctic psychrotroph Alteromonas haloplanctis A23.},
  author={Georges Feller and T Lonhienne and Christophe F. Deroanne and C{\'e}cile Libioulle and Jozef J. Van Beeumen and Charles Gerday},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 8},
  pages={5217-21}
}
The alpha-amylase excreted by the antarctic bacterium Alteromonas haloplanctis was purified and the corresponding amy gene was cloned and sequenced. N- and C-terminal amino acid sequencing were used to establish the primary structure of the mature A. haloplanctis alpha-amylase which is composed of 453 amino acids with a predicted Mr of 49,340 and a pI of 5.5. Three Ca2+ ions are bound per molecule and its activity is modulated by chloride ions. Within the four consensus sequences, Asp-174, Glu… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 67 extracted citations

Similar Papers

Loading similar papers…