title: The primary structure of Escherichia coli K12 aspartokinase I-homoserine dehydrogenase I. Site of limited proteolytic cleavage by subtilisin.
abstract: The sequence of the first 25 residues of the homoserine dehydrogenase fragment, produced by limited proteolysis of aspartokinase I-homoserine dehydrogenase I with substilisin, has been determined. The sequence of a cyanogen bromide peptide (CB5, 59 residues), isolated from the entire protein, is also presented. Residues 1 to 18 of the subtilisin homoserine dehydrogenase fragment match the sequence 42 to 59 of peptide CB5.
mesh_terms: D000595:Amino Acid Sequence; D001225:Aspartokinase Homoserine Dehydrogenase; D004926:Escherichia coli / Q000201:enzymology*; D009097:Multienzyme Complexes; D010446:Peptide Fragments / Q000032:analysis; D013381:Subtilisins
chemical_list: D009097:Multienzyme Complexes; D010446:Peptide Fragments; D001225:Aspartokinase Homoserine Dehydrogenase; D013381:Subtilisins