PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9108263-5	1997	In this study, we report the discovery and preliminary characterisation of a Z-Gly-Pro-NH-Mec-hydrolysing activity that is distinct from prolyl oligopeptidase (prolyl endopeptidase).	N-carbobenzoxyglycyl-prolyl-4-methylcoumarinyl amide	77-93	prolyl endopeptidase	Bos taurus	137-158	
9108263-5	1997	In this study, we report the discovery and preliminary characterisation of a Z-Gly-Pro-NH-Mec-hydrolysing activity that is distinct from prolyl oligopeptidase (prolyl endopeptidase).	N-carbobenzoxyglycyl-prolyl-4-methylcoumarinyl amide	77-93	prolyl endopeptidase	Bos taurus	160-180	
9108263-7	1997	In the presence of 350 nM Z-Pro-prolinal, a specific inhibitor of prolyl endopeptidase, residual Z-Gly-Pro-NH-Mec hydrolysis of 2.6 U/mg protein was observed.	N-carbobenzoxyglycyl-prolyl-4-methylcoumarinyl amide	97-113	prolyl endopeptidase	Bos taurus	66-86