Structure-based stabilization of an enzyme: the case of penicillin acylase from Alcaligenes faecalis.

@article{Wang2006StructurebasedSO,
  title={Structure-based stabilization of an enzyme: the case of penicillin acylase from Alcaligenes faecalis.},
  author={Tianwen David Wang and Hu Zhu and Xingyuan Ma and Yushu Ma and Dongzhi Wei},
  journal={Protein and peptide letters},
  year={2006},
  volume={13 2},
  pages={177-83}
}
The modeled structure of penicillin acylase from Alcaligenes faecali (AFPGA) was constructed by comparative modeling with the Modeller program. Candidate positions that could be replaced with cysteine were estimated by scanning the modeled structure of AFPGA with the program MODIP (modeling disulfide bond in protein). The mutant Q3C/P751C had a higher optimum temperature by three degrees than that of the wild type AFPGA. The half life of the double mutant Q3C/P751C at 55 degrees C was increased… CONTINUE READING