Sun K, Camardella L, Di Prisco G, Hervé G
Laboratoire de Biochimie des Signaux Régulateurs Cellulaires et Moléculaires, CNRS-UMR 7631, Université Pierre et Marie Curie, Paris, France.
FEMS Microbiol Lett. 1998 Jul 15;164(2):375-82. doi: 10.1111/j.1574-6968.1998.tb13112.x.
TAD1 is a psychrophilic strain isolated from continental frozen water in Antarctica. Study of aspartate transcarbamylase in the bacterium shows an impressive activity of this enzyme at low temperature. At 0 degree C, its activity is up to 26% of its maximal activity observed at 30 degrees C. In comparison with the Escherichia coli enzyme, some of its kinetic properties suggest that this high activity at low temperature results from an increased catalytic efficiency. This property might result from a discrete modification localized at the catalytic site, since this psychrophilic enzyme is as stable as its Escherichia coli homologue at high temperature.
TAD1是从南极洲大陆冷冻水中分离出的嗜冷菌株。对该细菌中天冬氨酸转氨甲酰酶的研究表明，这种酶在低温下具有令人印象深刻的活性。在0摄氏度时，其活性高达在30摄氏度时观察到的最大活性的26%。与大肠杆菌的酶相比，它的一些动力学特性表明，这种在低温下的高活性是由催化效率提高所致。由于这种嗜冷酶在高温下与其大肠杆菌同源物一样稳定，所以这种特性可能是由位于催化位点的离散修饰引起的。
