Properties of aspartate transcarbamylase from TAD1, a psychrophilic bacterial strain isolated from Antarctica

• Published in: FEMS Microbiology Letters
• Main Authors: Sun, Karine, Camardella, Laura, Di Prisco, Guido, Hervé, Guy
• Format: Text
• Language: English
• Published: Oxford University Press 1998
• Subjects: Articles; Antarc*; Antarctica
• Online Access: http://femsle.oxfordjournals.org/cgi/content/short/164/2/375; https://doi.org/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°C, its activity is up to 26% of its maximal activity observed at 30°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.