PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 7503422-3 1995 The results obtained with cathepsin A purified from human placenta demonstrate that the enzyme has the highest affinity for substrates with large hydrophobic (Phe, Leu) or positively charged (Arg) amino acid residues in P1" position. Leucine 164-167 cathepsin A Homo sapiens 26-37 34946974-5 2021 The polymorphism (85_87CTG>-) in exon 2 was a mutation causing a deletion of leucine, resulting in the change of the leucine 9-repeat (Leu9) to 8-repeat (Leu8) in the signal peptide region of CatA protein. Leucine 77-84 cathepsin A Homo sapiens 192-196 34946974-5 2021 The polymorphism (85_87CTG>-) in exon 2 was a mutation causing a deletion of leucine, resulting in the change of the leucine 9-repeat (Leu9) to 8-repeat (Leu8) in the signal peptide region of CatA protein. Leucine 117-124 cathepsin A Homo sapiens 192-196 9553770-8 1998 Whereas deamidase cleaves a variety of peptides with C-terminal or penultimate hydrophobic residues (e.g. substance P, angiotensin I, bradykinin, endothelin, fMet-Leu-Phe). Leucine 163-166 cathepsin A Homo sapiens 8-17