Purification and characterization of a cold-adapted isocitrate lyase and expression analysis of the cold-inducible isocitrate lyase gene from the psychrophilic bacterium Colwellia psychrerythraea.

@article{citeulike:2707527, abstract = {Isocitrate lyase (ICL) from Colwellia psychrerythraea, a psychrophilic bacterium, was purified and characterized. The subunit molecular mass was 64 kDa, which is larger than that of other bacterial ICLs. The optimal temperature for its activity was 25 degrees C, the value of K(m) for the substrate ( DL-isocitrate) was minimum at 15 degrees C, and the catalytic efficiency ( k(cat)/ K(m)) value was maximum at 20 degrees C. Furthermore, the enzyme was remarkably thermolabile and completely inactivated by incubation for 2 min at 30 degrees C. These features indicate that ICL from this bacterium is a typical cold-adapted enzyme. A partial amino acid sequence of the C. psychrerythraea ICL was very similar to that of the closely related psychrophile Colwellia maris. Expression of the gene encoding the C. psychrerythraea ICL was found to be induced by low temperatures and by acetate in the medium. The cold adaptation of the catalytic properties of ICL and the stimulated expression of its gene at low temperatures strongly suggest that this enzyme is important for the growth of this bacterium in a cold environment.}, address = {Division of Biological Sciences, Graduate School of Science, Hokkaido University, Kita 10-jo Nishi 8-chome, Kita-ku, Sapporo 060-0810, Japan.}, author = {Watanabe, S. and Yamaoka, N. and Fukunaga, N. and Takada, Y. }, citeulike-article-id = {2707527}, doi = {10.1007/s00792-002-0271-x}, issn = {1431-0651}, journal = {Extremophiles : life under extreme conditions}, keywords = {cold-adaptation}, month = {October}, number = {5}, pages = {397--405}, posted-at = {2008-04-23 13:52:20}, priority = {2}, title = {Purification and characterization of a cold-adapted isocitrate lyase and expression analysis of the cold-inducible isocitrate lyase gene from the psychrophilic bacterium Colwellia psychrerythraea.}, url = {http://dx.doi.org/10.1007/s00792-002-0271-x}, volume = {6}, year = {2002} }

TY - JOUR ID - citeulike:2707527 L3 - citeulike-article-id:2707527 TI - Purification and characterization of a cold-adapted isocitrate lyase and expression analysis of the cold-inducible isocitrate lyase gene from the psychrophilic bacterium Colwellia psychrerythraea. JF - Extremophiles : life under extreme conditions VL - 6 IS - 5 SP - 397 EP - 405 AD - Division of Biological Sciences, Graduate School of Science, Hokkaido University, Kita 10-jo Nishi 8-chome, Kita-ku, Sapporo 060-0810, Japan. SN - 1431-0651 N2 - Isocitrate lyase (ICL) from Colwellia psychrerythraea, a psychrophilic bacterium, was purified and characterized. The subunit molecular mass was 64 kDa, which is larger than that of other bacterial ICLs. The optimal temperature for its activity was 25 degrees C, the value of K(m) for the substrate ( DL-isocitrate) was minimum at 15 degrees C, and the catalytic efficiency ( k(cat)/ K(m)) value was maximum at 20 degrees C. Furthermore, the enzyme was remarkably thermolabile and completely inactivated by incubation for 2 min at 30 degrees C. These features indicate that ICL from this bacterium is a typical cold-adapted enzyme. A partial amino acid sequence of the C. psychrerythraea ICL was very similar to that of the closely related psychrophile Colwellia maris. Expression of the gene encoding the C. psychrerythraea ICL was found to be induced by low temperatures and by acetate in the medium. The cold adaptation of the catalytic properties of ICL and the stimulated expression of its gene at low temperatures strongly suggest that this enzyme is important for the growth of this bacterium in a cold environment. KW - cold-adaptation AU - Watanabe, S AU - Yamaoka, N AU - Fukunaga, N AU - Takada, Y PY - 2002/10// UR - http://dx.doi.org/10.1007/s00792-002-0271-x ER -