Two regions of the bifunctional protein aspartokinase I- homoserine dehydrogenase I are connected by a short hinge.
Four proteases differing in their specificity, i.e. subtilisin, trypsin, alpha-chymotrypsin and V8 staphylococcal protease, cleave the bifunctional protein Escherichia coli aspartokinase I-homoserine dehydrogenase I (composed of 820 residues) producing an active homoserine dehydrogenase fragment. This cleavage occurs within a short segment of the polypeptide chain extending from residue 293 to residue 300.
D000595:Amino Acid Sequence; D001225:Aspartokinase Homoserine Dehydrogenase; D002918:Chymotrypsin; D010450:Endopeptidases; D004926:Escherichia coli / Q000201:enzymology*; D009097:Multienzyme Complexes; D010446:Peptide Fragments / Q000032:analysis; D012697:Serine Endopeptidases; D013381:Subtilisins; D014357:Trypsin
D009097:Multienzyme Complexes; D010446:Peptide Fragments; D001225:Aspartokinase Homoserine Dehydrogenase; D010450:Endopeptidases; D012697:Serine Endopeptidases; D013381:Subtilisins; D002918:Chymotrypsin; C028344:glutamyl endopeptidase; D014357:Trypsin