Mechanistic analysis of the phosphonate transition-state analogue-derived catalytic and non-catalytic antibody.

@article{Nishi2007MechanisticAO,
  title={Mechanistic analysis of the phosphonate transition-state analogue-derived catalytic and non-catalytic antibody.},
  author={Yoshisuke Nishi and Naoki Yamamoto and Kazuko Shimazaki and Naoko Takahashi-Ando and Hiroyuki Kakinuma and Sun Jialin and Sergey N Ruzheinikov and Tatyana A Muranova and David W. Rice and Yasuhiro Kajihara},
  journal={Journal of biochemistry},
  year={2007},
  volume={142 4},
  pages={421-33}
}
The esterolytic catalytic antibody (catAb) has the positive charged region interacting with the carbonyl group of the ester substrate. To examine how such a region interacts with the substrate, we compared the catAb with the non-catalytic antibody (non-catAb) for interaction with the non-cleavable amide substrate (a mimic of the ester substrate) and the two… CONTINUE READING