Improving the activity and stability of GL-7-ACA acylase CA130 by site-directed mutagenesis.

@article{Zhang2005ImprovingTA,
  title={Improving the activity and stability of GL-7-ACA acylase CA130 by site-directed mutagenesis.},
  author={Wei Zhang and Yuan Liu and Huabao Zheng and Sheng Yang and Wei-hong Jiang},
  journal={Applied and environmental microbiology},
  year={2005},
  volume={71 9},
  pages={5290-6}
}
In the present study, glutaryl-7-amino cephalosporanic acid acylase from Pseudomonas sp. strain 130 (CA130) was mutated to improve its enzymatic activity and stability. Based on the crystal structure of CA130, two series of amino acid residues, one from those directly involved in catalytic function and another from those putatively involved in surface charge, were selected as targets for site-directed mutagenesis. In the first series of experiments, several key residues in the substrate-binding… CONTINUE READING
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