Properties of aspartate transcarbamylase from TAD1, a psychrophilic bacterial strain isolated from Antarctica.
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.
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Laboratoire de Biochimie des Signaux Régulateurs Cellulaires et Moléculaires, CNRS-UMR 7631, Université Pierre et Marie Curie, Paris, France.
Camardella
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Di Prisco
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Hervé
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D000864:Antarctic Regions; D001221:Aspartate Carbamoyltransferase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism*; D002221:Carbamyl Phosphate / Q000378:metabolism; D006090:Gram-Negative Bacteria / Q000201:enzymology* / Q000254:growth & development / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D007053:Ice; D007700:Kinetics; D009711:Nucleotides / Q000378:metabolism; D012623:Seawater / Q000382:microbiology*; D013696:Temperature
D007053:Ice; D009711:Nucleotides; D002221:Carbamyl Phosphate; D001221:Aspartate Carbamoyltransferase