Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography.

@article{Yamaguchi2005ProbingTR,
  title={Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography.},
  author={Yoshihiro Yamaguchi and Takahiro Kuroki and Hisami Yasuzawa and Toshihiro Higashi and Wanchun Jin and Akiko Kawanami and Yuriko Yamagata and Yoshichika Arakawa and Masafumi Goto and Hiromasa Kurosaki},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 21},
  pages={20824-32}
}
Metallo-beta-lactamase IMP-1 is a di-Zn(II) metalloenzyme that efficiently hydrolyzes beta-lactam antibiotics. Wild-type (WT) IMP-1 has a conserved Asp-120(81) in the active site, which plays an important role in catalysis. To probe the catalytic role of Asp-120(81) in IMP-1, the IMP-1 mutants, D120(81)A and D120(81)E, were prepared by site-directed… CONTINUE READING