E. coli aspartokinase II-homoserine dehydrogenase II polypeptide chain has a triglobular structure.
E.coli aspartokinase II-homoserine dehydrogenase II is, as aspartokinase I-homoserine dehydrogenase I, composed of three globular domains: the N-terminal domain is endowed with kinase activity; the C-terminal domain carries the dehydrogenase activity. These two parts of the polypeptide chain are separated by a central inactive domain. Thus, the polypeptide chains of the two multifunctional proteins are homologous not only in their sequence but also in their triglobular domain structure.
D001225:Aspartokinase Homoserine Dehydrogenase / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D046911:Macromolecular Substances; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis; D011402:Pronase; D011487:Protein Conformation
D046911:Macromolecular Substances; D009097:Multienzyme Complexes; D010446:Peptide Fragments; D001225:Aspartokinase Homoserine Dehydrogenase; D011402:Pronase