Properties and chemical modification of D-amino acid oxidase from Trigonopsis variabilis

@article{Schrder1996PropertiesAC,
  title={Properties and chemical modification of D-amino acid oxidase from Trigonopsis variabilis},
  author={Thomas Schr{\"a}der and Jan Remmer Andreesen},
  journal={Archives of Microbiology},
  year={1996},
  volume={165},
  pages={41-47}
}
The basic properties of purified d-amino acid oxidase from the yeast Trigonopsis variabilis were investigated. The pH optimum of activity was between pH 8.5 and 9.0, and the native molecular masses of holo- and apo-enzyme were determined to be 170 kDa; higher aggregates corresponded to molecular masses of 320 and 570 kDa. The apparent V max and K m values for different substrates varied between 3.7 to 185 U/mg and 0.2 to 17.3 mM, respectively. The reaction of d-amino acid oxidase with sulfite… CONTINUE READING

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