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- W1594559208 abstract "Abstract Arginine-inducible acetylornithine δ-transaminase, which catalyzes the reversible conversion of N-acetylglutamic γ-semialdehyde and l-glutamate to α-N-acetyl-l-ornithine and α-ketoglutarate, has been isolated in homogeneous form, as judged by disc gel electrophoresis, immunoelectrophoresis, and ultracentrifugation. A double mutant of Escherichia coli strain W which lacks arginine-repressible acetylornithine δ-transaminase was used as the source of aminotransferase. In the assay used, optimal enzymatic activity occurs at pH 7.8, and requires the addition of pyridoxal 5-phosphate. The activity was measured in the reverse of the biosynthetic reaction and, under this condition, only α-N-acetyl-l-ornithine and α-ketoglutarate were found to serve as substrates. A number of divalent cations tested do not affect the activity of the enzyme, with the exception of Cu++ and Hg++, which are inhibitory. From amino acid analysis, the enzyme contains 5 half-cystine residues per molecule, and a partial specific volume of 0.734 has been calculated. The average molecular weight of acetylornithine δ-transaminase, based upon sedimentation equilibrium data, is 61,000, and an s020,w of 4.6 has been determined." @default.
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- W1594559208 date "1970-10-01" @default.
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- W1594559208 title "Isolation and Characterization of Arginine-inducible Acetylornithine δ-Transaminase from Escherichia coli" @default.
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- W1594559208 doi "https://doi.org/10.1016/s0021-9258(18)62762-0" @default.
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