The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: a molecular modelling study.
Based on molecular modelling study, we propose that the reaction between L-aspartate an carbamoylphosphate, catalyzed by E. coli aspartate carbamoyltransferase, may proceed via a tetrahedral intermediate and that the breakdown of the intermediate is facilitated by an intramolecular proton transfer between the amino group of L-aspartate and a terminal phosphate oxygen of carbamoylphosphate.
D001221:Aspartate Carbamoyltransferase / Q000378:metabolism*; D001224:Aspartic Acid / Q000031:analogs & derivatives / Q000378:metabolism; D001665:Binding Sites; D002221:Carbamyl Phosphate / Q000378:metabolism; D055598:Chemical Phenomena; D002621:Chemistry; D004926:Escherichia coli / Q000201:enzymology*; D006860:Hydrogen Bonding; D008956:Models, Chemical; D008968:Molecular Conformation; D010746:Phosphonoacetic Acid / Q000031:analogs & derivatives / Q000378:metabolism
D001224:Aspartic Acid; D002221:Carbamyl Phosphate; C013195:sparfosic acid; D001221:Aspartate Carbamoyltransferase; D010746:Phosphonoacetic Acid