Procedures that have been developed for the purification of acetylornithine δ transaminase from E. coli W also lead to the simultaneous purification of ornithine δ transaminase. These 2 enzymatic activities have the same electrophoretic mobility and are identical immunochemically. Studies of inhibition kinetics demonstrate that the 2 substrates, acetylornithine and ornithine, compete for the same active site of acetylornithine δ transaminase; thus, the ornithine δ transaminase activity in E. coli is due to acetylornithine δ transaminase and not to a separate specific ornithine δ transaminase.
CITATION STYLE
Billhemier, J. T., Carnevale, H. N., Leisinger, T., Eckhardt, T., & Jones, E. E. (1976). Ornithine δ transaminase activity in Escherichia coli: Its identity with acetylornithine δ transaminase. Journal of Bacteriology, 127(3), 1315–1323. https://doi.org/10.1128/jb.127.3.1315-1323.1976
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