The effect of deleting a putative salt bridge on the properties of the thermostable subtilisin-like proteinase, aqualysin I.

@article{Arnrsdttir2011TheEO,
  title={The effect of deleting a putative salt bridge on the properties of the thermostable subtilisin-like proteinase, aqualysin I.},
  author={J{\'o}hanna Arn{\'o}rsd{\'o}ttir and Manuela Magn{\'u}sd{\'o}ttir and Olafur H Friđj{\'o}nsson and Magn{\'u}s M Kristj{\'a}nsson},
  journal={Protein and peptide letters},
  year={2011},
  volume={18 6},
  pages={545-51}
}
Aqualysin I, is a subtilisin-like serine proteinase, from the thermophilic bacterium Thermus aquaticus. It is predicted that the enzyme contains a salt bridge, D17-R259, connecting the N- and C-terminal regions of the enzyme. Previously we reported on the stabilizing effect of the incorporation of a salt bridge at a corresponding site in VPR, a related cold adapted enzyme from a marine Vibrio sp. Here we describe the effect of the reverse change, i.e. the elimination of the salt bridge on the… CONTINUE READING