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open-access-imgOpen AccessOrnithine delta-transaminase activity in Escherichia coli: its identity with acetylornithine delta-transaminase
J T Billhemier,
Helen N. Carnevale,
Thomas Leisinger,
T Eckhardt,
E E Jones
Publication year1976
Publication title
journal of bacteriology
Resource typeJournals
PublisherAmerican Society for Microbiology
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.
Subject(s)aerospace engineering , alanine transaminase , alkaline phosphatase , amino acid , arginine , aspartate transaminase , biochemistry , biology , delta , endocrinology , engineering , enzyme , escherichia coli , gene , ornithine , transaminase
SCImago Journal Rank1.652

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