Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning.

@article{Asano1987PhenylalanineDO,
  title={Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning.},
  author={Yasuhisa Asano and Asako Nakazawa and Kohki Endo and Yasuhide Hibino and Masayuki Ohmori and Naganori Numao and Kumiko Kondo},
  journal={European journal of biochemistry},
  year={1987},
  volume={168 1},
  pages={
          153-9
        }
}
Phenylalanine dehydrogenase produced by Bacillus badius IAM 11059 was purified from the crude extract of B. badius to homogeneity, as judged by disc gel electrophoresis. The enzyme has an isoelectric point of 3.5 and a relative molecular mass, Mr, of 310,000-360,000. The enzyme is composed of identical subunits with an Mr 41,000-42,000. The substrate specificity of the enzyme in the oxidative deamination reaction was high for L-phenylalanine, but rather low in the reductive amination reaction… CONTINUE READING

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Methods of enzymatic analysis 2nd edn, vol. 1 (Bergmeyer

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