Isolation of the aspartokinase domain of bifunctional aspartokinase I-homoserine dehydrogenase I from E.coli K12.
A proteolytic fragment (Mr approximately 25 000) carrying only the aspartokinase activity has been purified by chromatofocusing after limited proteolysis of aspartokinase I-homoserine dehydrogenase I from E.coli K12. The NH2-terminal sequence shows that it corresponds to the amino terminal peptide of the native enzyme. The results confirm a previous hypothesis about the organization of native aspartokinase I-homoserine dehydrogenase I.
Veron
M
M
Guillou
Y
Y
Cohen
G N
GN
D000595:Amino Acid Sequence; D001222:Aspartate Kinase / Q000302:isolation & purification*; D001225:Aspartokinase Homoserine Dehydrogenase / Q000032:analysis*; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000032:analysis*; D010446:Peptide Fragments / Q000302:isolation & purification; D010770:Phosphotransferases / Q000302:isolation & purification*; D011402:Pronase / Q000378:metabolism
D009097:Multienzyme Complexes; D010446:Peptide Fragments; D010770:Phosphotransferases; D001222:Aspartate Kinase; D001225:Aspartokinase Homoserine Dehydrogenase; D011402:Pronase