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

Author:

Billhemier J T,Carnevale H N,Leisinger T,Eckhardt T,Jones E E

Abstract

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.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference22 articles.

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4. The kinetics of enzyme-catalyzed reactions with two or more substrates or products. III. Prediction of initial velocity and inhibition patterns by inspection;Cleland W. W.;Biochim. Biophys. Acta,1963

5. The genetic control of the arginine pathways in Aspergillus nidulans mutants blocked in arginine biosynthesis;Cybis J.;Acta Microbiol. Pol. Ser. A,1972

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