Ordered substrate binding and evidence for a thermally induced change in mechanism for E. coli aspartate transcarbamylase.
D001221:Aspartate Carbamoyltransferase / Q000378:metabolism*; D001224:Aspartic Acid; D001665:Binding Sites; D002151:Calorimetry; D002219:Carbamates; D002250:Carbon Radioisotopes; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli / Q000201:enzymology*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D007553:Isotope Labeling; D007700:Kinetics; D008433:Mathematics; D009943:Organophosphorus Compounds; D010761:Phosphorus Radioisotopes; D011485:Protein Binding; D013696:Temperature; D013816:Thermodynamics; D013997:Time Factors
D002219:Carbamates; D002250:Carbon Radioisotopes; D009943:Organophosphorus Compounds; D010761:Phosphorus Radioisotopes; D001224:Aspartic Acid; D001221:Aspartate Carbamoyltransferase