| Literature DB >> 8431 |
J T Billheimer, H N Carnevale, T Leisinger, T Eckhardt, E E Jones.
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.Entities:
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Year: 1976 PMID: 8431 PMCID: PMC232926 DOI: 10.1128/jb.127.3.1315-1323.1976
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490