Ornithine delta-transaminase activity in Escherichia coli: its identity with acetylornithine delta-transaminase.

AUTOR(ES)

Billhemier, J T

RESUMO

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.

Documentos Relacionados

• Regulation of Transaminase C Synthesis in Escherichia coli: Conditional Leucine Auxotrophy
• Pseudouridylate Synthetase of Escherichia coli: Correlation of Its Activity with Utilization of Pseudouridine for Growth
• Occurrence of Hydroxypyruvate—l-Glutamate Transaminase in Escherichia coli and Its Separation from Hydroxypyruvate-Phosphate—l-Glutamate Transaminase
• Transaminase B from Escherichia coli: Quaternary Structure, Amino-Terminal Sequence, Substrate Specificity, and Absence of a Separate Valine-α-Ketoglutarate Activity†
• Activity of flumequine against Escherichia coli: in vitro comparison with nalidixic and oxolinic acids.