The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral proteinase.

@article{Sidler1986ThePS,
  title={The primary structure of Bacillus cereus neutral proteinase and comparison with thermolysin and Bacillus subtilis neutral proteinase.},
  author={Walter Sidler and Eva M. Niederer and Fabian Suter and Herbert Zuber},
  journal={Biological chemistry Hoppe-Seyler},
  year={1986},
  volume={367 7},
  pages={
          643-57
        }
}
The complete amino-acid sequence of a neutral proteinase, produced by Bacillus cereus, was determined by protein sequencing. The neutral proteinase consists of 317 amino-acid residues. The primary structure is 70% homologous to thermolysin, a thermostable neutral proteinase and 45% homologous to Bacillus subtilis neutral proteinase. The zinc-binding site and the hydrophobic pocket of the active site are highly similar in all three proteinases. B. cereus neutral proteinase which is 20 degrees C… CONTINUE READING

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