Relationship between an increase in thermostability and amino acid substitutions in N-carbamyl-D-amino acid amidohydrolase.

@article{Ikenaka1998RelationshipBA,
  title={Relationship between an increase in thermostability and amino acid substitutions in N-carbamyl-D-amino acid amidohydrolase.},
  author={Yasuhiro Ikenaka and Hirokazu Nanba and Kanako Yajima and Yoichi Yamada and Mutsumi Takano and Saori Takahashi},
  journal={Bioscience, biotechnology, and biochemistry},
  year={1998},
  volume={62 9},
  pages={1672-5}
}
For the production of D-amino acids using stable N-carbamyl-D-amino acid amidohydrolase (DCase) in an immobilized form, the DCase gene of Agrobacterium sp. KNK712 was mutagenized to increase its enzymatic thermostability. In a search for thermostability-related amino acid sites besides the two known sites of DCase, i.e., the 57th and 203rd amino acids, the new mutant enzyme found, in which the 236th amino acid, valine, had been changed to alanine, showed a 10 degrees C increase in… CONTINUE READING

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