Endothiapepsin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.23 Aspartic endopeptidases > 3.4.23.22 Endothiapepsin
Endothiapepsin is an aspartic endopeptidase from the ascomycete Endothia parasitica, belonging to peptidase family A1. Like pepsin A it hydrolyzes proteins, preferring hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the insulin B chain or Z-Glu-Tyr; it clots milk. In the fungus it digests extracellular proteins and is widely used as a structural model for aspartic proteases. It features a pepsin-like aspartic-protease fold.
Endothiapepsin is an aspartic endopeptidase from the ascomycete Endothia parasitica, belonging to peptidase family A1. Like pepsin A it hydrolyzes proteins, preferring hydrophobic residues at P1 and P1', but does not cleave Ala14-Leu in the insulin B chain or Z-Glu-Tyr; it clots milk. In the fungus it digests extracellular proteins and is widely used as a structural model for aspartic proteases. It features a pepsin-like aspartic-protease fold.
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