Ornithine delta-transaminase activity in Escherichia coli: its identity with acetylornithine delta-transaminase.
Procedures that have been developed for the purification of acetylornithine delta-transaminase from Escherichia coli W also lead to the simultaneous purification of ornithine delta-transaminase. These two enzymatic activities have the same electrophoretic mobility and are identical immunochemically. Studies of inhibition kinetics demonstrate that the two substrates, acetylornithine and ornithine, compete for the same active site of acetylornithine delta-transaminase; thus, the ornithine delta-transaminase activity in E coli is due to acetylornithine delta-transaminase and not to a separate specific ornithine delta-transaminase.
D001665:Binding Sites; D004589:Electrophoresis, Disc; D004790:Enzyme Induction; D004794:Enzyme Repression; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007118:Immunoassay; D007700:Kinetics; D009953:Ornithine-Oxo-Acid Transaminase / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*; D000637:Transaminases / Q000096:biosynthesis / Q000302:isolation & purification / Q000378:metabolism*
D000637:Transaminases; D009953:Ornithine-Oxo-Acid Transaminase