Revisiting the allosteric mechanism of aspartate transcarbamoylase.
Fetler
Luc
L
LURE (CNRS, CEA, MER), Bâtiment 209D, B.P. 34, Université Paris-Sud, 91898 Orsay Cedex, France. luc.fetler@curie.fr
Vachette
Patrice
P
D000494:Allosteric Regulation; D000495:Allosteric Site; D001221:Aspartate Carbamoyltransferase / Q000737:chemistry / Q000378:metabolism*; D001224:Aspartic Acid / Q000031:analogs & derivatives* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D010746:Phosphonoacetic Acid / Q000031:analogs & derivatives* / Q000378:metabolism; D011487:Protein Conformation; D013816:Thermodynamics; D014961:X-Ray Diffraction
D001224:Aspartic Acid; C013195:sparfosic acid; D001221:Aspartate Carbamoyltransferase; D010746:Phosphonoacetic Acid