Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands.
D001224:Aspartic Acid; D001565:Benzoates; D001665:Binding Sites; D002384:Catalysis; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003597:Cytosine Nucleotides; D004926:Escherichia coli / Q000201:enzymology*; D005246:Feedback; D007700:Kinetics; D008628:Mercury; D013053:Spectrophotometry; D013386:Succinates; D013438:Sulfhydryl Compounds; D014166:Transferases / Q000037:antagonists & inhibitors
D001565:Benzoates; D003597:Cytosine Nucleotides; D013386:Succinates; D013438:Sulfhydryl Compounds; D001224:Aspartic Acid; D014166:Transferases; D008628:Mercury