Enhancement of catalytic efficiency by the combination of site-specific mutations in a carbonic anhydrase-related protein.

@article{Elleby2000EnhancementOC,
  title={Enhancement of catalytic efficiency by the combination of site-specific mutations in a carbonic anhydrase-related protein.},
  author={B Elleby and Bj{\"o}rn Sj{\"o}blom and Chingkuang Tu and David N. Silverman and Sven Lindskog},
  journal={European journal of biochemistry},
  year={2000},
  volume={267 19},
  pages={5908-15}
}
A single mutation, involving the replacement of an arginine residue with histidine to reconstruct a zinc-binding site, suffices to change a catalytically inactive murine carbonic anhydrase-related protein (CARP) to an active carbonic anhydrase with a CO2-hydration turnover number of 1.2 x 104 s-1. Further mutations, leading to a more 'carbonic anhydrase-like' active-site cavity, results in increased activity. A quintuple mutant having His94, Gln92, Val121, Val143, and Thr200 (human carbonic… CONTINUE READING