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

J T Billhemier | Zendy; Helen N. Carnevale | Zendy; Thomas Leisinger | Zendy; Thomas Eckhardt | Zendy; Evan E. Jones | Zendy

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

Author(s) -

J T Billhemier,

Helen N. Carnevale,

Thomas Leisinger,

Thomas Eckhardt,

Evan E. Jones

Publication year - 1976

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.127.3.1315-1323.1976

Subject(s) - transaminase , biology , ornithine , biochemistry , escherichia coli , aspartate transaminase , delta , arginine , alanine transaminase , enzyme , amino acid , alkaline phosphatase , endocrinology , gene , engineering , aerospace engineering

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.

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