Unique catalytic and molecular properties of hydrolases from Aspergillus used in Japanese bioindustries.

@article{Ichishima2000UniqueCA,
  title={Unique catalytic and molecular properties of hydrolases from Aspergillus used in Japanese bioindustries.},
  author={Eiji Ichishima},
  journal={Bioscience, biotechnology, and biochemistry},
  year={2000},
  volume={64 4},
  pages={675-88}
}
  • Eiji Ichishima
  • Published 2000 in Bioscience, biotechnology, and biochemistry
This review covers the unique catalytic and molecular properties of three proteolytic enzymes and a glycosidase from Aspergillus. An aspartic proteinase from A. saitoi, aspergillopepsin I (EC 3.4.23.18), favors hydrophobic amino acids at P1 and P'1 like gastric pepsin. However, aspergillopepsin I accommodates a Lys residue at P1, which leads to activation of trypsinogens like duodenum enteropeptidase. Substitution of Asp76 to Ser or Thr and deletion of Ser78, corresponding to the mammalian… CONTINUE READING
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