Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptides, including enkephalin-containing peptides.

@article{Orlowski1989Endopeptidase2F,
  title={Endopeptidase 24.15 from rat testes. Isolation of the enzyme and its specificity toward synthetic and natural peptides, including enkephalin-containing peptides.},
  author={Marian Orlowski and Shlomo Reznik and Juan Alfonso Ayala and Adrian Ronald Pierotti},
  journal={The Biochemical journal},
  year={1989},
  volume={261 3},
  pages={
          951-8
        }
}
Endopeptidase 24.15, a metalloendopeptidase (EC 3.4.24.15) with an Mr of about 70,000, was purified to homogeneity from rat testes. The enzyme cleaves preferentially bonds on the carboxyl side of hydrophobic amino acids. Secondary enzyme-substrate interactions at sites removed from the scissile bond are indicated by the finding that a hydrophobic or bulky residue in the P3' position greatly contributes to substrate binding and catalytic efficiency. The isolated enzyme is inhibited by metal… CONTINUE READING
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