PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
1312513-4	1992	The most potent converting enzyme inhibitors toward aminopeptidase P were the carboxylalkyl compounds, cilazaprilat, enalaprilat, and ramiprilat (I50 values of 3-12 microM).	carboxylalkyl compounds	78-101	X-prolyl aminopeptidase 2	Sus scrofa	52-68
6298420-2	1983	Differential recognition of both brain enkephalinase and angiotensin-converting enzyme (ACE) catalytic sites by these carboxylalkyl compounds lead to potent (KI approximately 0.5 microM), competitive and selective inhibitors of the enkephalin-degrading enzyme.	carboxylalkyl compounds	118-141	angiotensin I converting enzyme (peptidyl-dipeptidase A) 1	Mus musculus	57-86
6298420-2	1983	Differential recognition of both brain enkephalinase and angiotensin-converting enzyme (ACE) catalytic sites by these carboxylalkyl compounds lead to potent (KI approximately 0.5 microM), competitive and selective inhibitors of the enkephalin-degrading enzyme.	carboxylalkyl compounds	118-141	angiotensin I converting enzyme (peptidyl-dipeptidase A) 1	Mus musculus	88-91