Hydroperoxidase II of Escherichia coli exhibits enhanced resistance to proteolytic cleavage compared to other catalases.

@article{Chelikani2003HydroperoxidaseIO,
  title={Hydroperoxidase II of Escherichia coli exhibits enhanced resistance to proteolytic cleavage compared to other catalases.},
  author={Prashen Chelikani and Lynda J. Donald and Harry W. Duckworth and Peter C Loewen},
  journal={Biochemistry},
  year={2003},
  volume={42 19},
  pages={5729-35}
}
Catalase (hydroperoxidase) HPII of Escherichia coli is the largest catalase so far characterized, existing as a homotetramer of 84 kDa subunits. Each subunit has a core structure that closely resembles small subunit catalases, supplemented with an extended N-terminal sequence and compact flavodoxin-like C-terminal domain. Treatment of HPII with trypsin, chymotrypsin, or proteinase K, under conditions of limited digestion, resulted in cleavage of 72-74 residues from the N-terminus of each… CONTINUE READING