[en] A cold-active alpha-amylase was purified from culture supernatants of the antarctic psychrophile Alteromonas haloplanctis A23 grown at 4 degrees C. In order to contribute to the understanding of the molecular basis of cold adaptations, crystallographic studies of this cold-adapted enzyme have been initiated because a three-dimensional structure of a mesophilic counterpart, pig pancreatic alpha-amylase, already exists. alpha-Amylase from A. haloplanctis, which shares 53% sequence identity with pig pancreatic alpha-amylase, has been crystallized and data to 1.85 A have been collected. The space group is found to be C222(1) with a = 71.40 A, b = 138.88 A, and c = 115.66 A. Until now, a three-dimensional structure of a psychrophilic enzyme is lacking.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Aghajari, N.
Feller, Georges ; Université de Liège - ULiège > Département des sciences de la vie > Labo de biochimie
Gerday, Charles ; Université de Liège - ULiège > Services généraux (Faculté des sciences) > Relations académiques et scientifiques (Sciences)
Haser, R.
Language :
English
Title :
Crystallization and preliminary X-ray diffraction studies of a-amylase from the antarctic psychrophile Alteromonas haloplanctis A23
Publication date :
1996
Journal title :
Protein Science: A Publication of the Protein Society
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