L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition.

@article{Mortarino1996LaspartateOF,
  title={L-aspartate oxidase from Escherichia coli. I. Characterization of coenzyme binding and product inhibition.},
  author={Michele Mortarino and Armando Negri and Gabriellla Tedeschi and Tatjana Simonic and Stefano Duga and Hans G{\"u}nter Gassen and Silvia Ronchi},
  journal={European journal of biochemistry},
  year={1996},
  volume={239 2},
  pages={418-26}
}
This paper reports the biochemical characterization of the flavoprotein L-aspartate oxidase from Escherichia coli. Modification of a previously published procedure allowed overexpression of the holoenzyme in an unproteolysed form. L-Aspartate oxidase is a monomer of 60 kDa containing 1 mol of noncovalently bound FAD/mol protein. A polarographic and two spectrophotometric coupled assays have been set up to monitor the enzymatic activity continuously. L-Aspartate oxidase was subjected to product… CONTINUE READING
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