title: Specificity of rat liver cathepsin D.
abstract: The specificity of highly purified rat liver cathepsin D was investigated by analyzing the digests of denatured proteins. At the P1 site, cathepsin D prefers hydrophobic residues except Ile and Val, that are branched at the beta-carbon. Strong and weak hydrophobicities are required at P1' and P2 sites, respectively. A lower protency for beta-turn formation is essential for the sequence around the P1 site.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002402:Cathepsin D / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D011489:Protein Denaturation; D051381:Rats; D013379:Substrate Specificity
chemical_list: D002402:Cathepsin D