Cathepsin D
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.23 Aspartic endopeptidases > 3.4.23.5 cathepsin D
Cathepsin D is an intracellular lysosomal aspartic endopeptidase with a known zymogen form, in peptidase family A1. Its specificity is similar to but narrower than pepsin A, and it does not cleave the Gln4-His bond in the insulin B chain. In lysosomes it degrades endocytosed and autophagocytosed proteins; when missecreted it contributes to extracellular matrix remodeling and cancer invasion. It features a pepsin-like aspartic-protease fold.
Cathepsin D is an intracellular lysosomal aspartic endopeptidase with a known zymogen form, in peptidase family A1. Its specificity is similar to but narrower than pepsin A, and it does not cleave the Gln4-His bond in the insulin B chain. In lysosomes it degrades endocytosed and autophagocytosed proteins; when missecreted it contributes to extracellular matrix remodeling and cancer invasion. It features a pepsin-like aspartic-protease fold.
References:
Biomedical Dictionary
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