PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21921028-2	2011	Since that time, seven additional mammalian members of the CPA subfamily have been described, all of which are initially produced as proenzymes, are activated by endoproteases, and remove either C-terminal hydrophobic or basic amino acids from peptides.	Peptides	244-252	carboxypeptidase A1	Homo sapiens	59-62	
21921028-5	2011	CPO was purified by affinity chromatography, and the purified enzyme was able to cleave proteins and synthetic peptides with greatest activity toward acidic C-terminal amino acids unlike other CPA-like enzymes.	Peptides	111-119	carboxypeptidase O	Homo sapiens	0-3	
21921028-6	2011	CPO displayed a neutral pH optimum and was inhibited by common metallocarboxypeptidase inhibitors as well as citrate.	Citric Acid	109-116	carboxypeptidase O	Homo sapiens	0-3	
21921028-7	2011	CPO was modified by attachment of a glycosylphosphatidylinositol membrane anchor to the C terminus of the protein.	Glycosylphosphatidylinositols	36-64	carboxypeptidase O	Homo sapiens	0-3	
21921028-10	2011	These results suggest that CPO cleaves acidic amino acids from dietary proteins and peptides, thus complementing the actions of well known digestive carboxypeptidases CPA and CPB.	Acids	39-45	carboxypeptidase O	Homo sapiens	27-30	
21921028-10	2011	These results suggest that CPO cleaves acidic amino acids from dietary proteins and peptides, thus complementing the actions of well known digestive carboxypeptidases CPA and CPB.	Acids	39-45	carboxypeptidase A1	Homo sapiens	167-170	
21921028-10	2011	These results suggest that CPO cleaves acidic amino acids from dietary proteins and peptides, thus complementing the actions of well known digestive carboxypeptidases CPA and CPB.	cpb	175-178	carboxypeptidase O	Homo sapiens	27-30