PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21366335-3	2011	In alpha-amylases and ACE, removal of chloride from the binding site triggers formation of a salt bridge between the positively charged Arg or Lys residue involved in chloride binding and a nearby carboxylate residue.	carboxylate	197-208	angiotensin I converting enzyme	Homo sapiens	22-25	
2992465-2	1985	The hydrolysis of enkephalins and analogues was more affected by the nature of P1 and P2 residues in the case of thermolysin than in those of ACE or "enkephalinase"; amidation of the C-terminal carboxylate decreased drastically the hydrolysis by ACE but only marginally by thermolysin and the effect was intermediate for "enkephalinase".	carboxylate	194-205	angiotensin I converting enzyme	Homo sapiens	142-145	
10906415-1	2000	The alpha,beta-unsaturated amide that is incorporated into the basic structural frame of a simple substrate molecule of angiotensin converting enzyme was found to serve as a Michael acceptor for the catalytic carboxylate of Glu-127, inhibiting the enzyme irreversibly.	carboxylate	209-220	angiotensin I converting enzyme	Homo sapiens	120-149	
10698448-2	2000	Although compounds which inhibit the activity of both ACE and NEP (vasopeptidase inhibitors, VPIs) have been reported which incorporate a thiol, carboxylate, or phosphorus acid pharmacophore, the generation of hydroxamate based vasopeptidase inhibitors has remained elusive.	carboxylate	145-156	angiotensin I converting enzyme	Homo sapiens	54-57	
2485059-4	1987	These and more recently developed ACE inhibitors can be classified according to their structural analogy to dipeptides or tripeptides and according to the nature of their zinc-binding ligands, such as sulfhydryl, ketone, carboxylate, or hydroxyphosphinyl, that contribute greatly to their binding to ACE.	carboxylate	221-232	angiotensin I converting enzyme	Homo sapiens	34-37