Enhancement of oxidative stability of the subtilisin nattokinase by site-directed mutagenesis expressed in Escherichia coli.

@article{Weng2009EnhancementOO,
  title={Enhancement of oxidative stability of the subtilisin nattokinase by site-directed mutagenesis expressed in Escherichia coli.},
  author={Meizhi Weng and Zhongliang Zheng and Wei Bao and Yongjun Cai and Yan Yin and Guolin Zou},
  journal={Biochimica et biophysica acta},
  year={2009},
  volume={1794 11},
  pages={1566-72}
}
Nattokinase (subtilisin NAT, NK) is a bacterial serine protease with strong fibrinolytic activity and it is a potent cardiovascular drug. In medical and commercial applications, however, it is susceptible to chemical oxidation, and subsequent inactivation or denaturation. Here we show that the oxidative stability of NK was substantially increased by optimizing the amino acid residues Thr(220) and Met(222), which were in the vicinity of the catalytic residue Ser(221) of the enzyme. Two… CONTINUE READING
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