PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2924773-1	1989	Consideration of the active-site model of prolidase led us to examine azetidine, pyrrolidine and piperidine substrate analogs as potential in vivo inhibitors of the enzyme.	azetidine	70-79	peptidase D	Homo sapiens	42-51	
2924773-1	1989	Consideration of the active-site model of prolidase led us to examine azetidine, pyrrolidine and piperidine substrate analogs as potential in vivo inhibitors of the enzyme.	pyrrolidine	81-92	peptidase D	Homo sapiens	42-51	
2924773-1	1989	Consideration of the active-site model of prolidase led us to examine azetidine, pyrrolidine and piperidine substrate analogs as potential in vivo inhibitors of the enzyme.	piperidine	97-107	peptidase D	Homo sapiens	42-51	
2924773-2	1989	One of these, N-benzyloxycarbonyl-L-proline, was shown to be a potent competitive inhibitor of porcine kidney prolidase (Ki = 90 microM); its rapid protein-mediated permeation of human and sheep erythrocytes suggests that it may be effective in vivo.	carbobenzoxyproline	14-43	peptidase D	Homo sapiens	110-119	
2924773-4	1989	Analysis of inhibitor action and consideration of X-ray crystallographic data of relevant Mn2+ complexes allowed the active-site model of prolidase to be further refined; a new model is presented in which the substrate acts as a bidentate ligand towards the active-site manganous ion.	Manganese(2+)	90-94	peptidase D	Homo sapiens	138-147