PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3922786-1	1985	The reaction of porcine pancreatic lipase with an organophosphorus compound bis-p-nitrophenyl methylphosphonate (BNMP) resulted in the complete and irreversible inhibition of lipase activity on tributyrin emulsion (25 degrees C, pH 7.5, 40 mM Na-veronal-HCl buffer) whereas the activity of the enzyme on p-nitrophenyl acetate solution remained unchanged.	4-nitrophenyl acetate	304-325	pancreatic lipase	Homo sapiens	24-41	
990257-3	1976	Hydrolysis of dissolved p-nitrophenyl acetate by pancreatic lipase follows the classical acyl enzyme pathway already proposed for other esterases.	4-nitrophenyl acetate	24-45	pancreatic lipase	Homo sapiens	49-66	
990257-10	1976	Hydrolysis by pancreatic lipase of dissolved monomeric p-nitrophenyl acetate and triacetin is considerably enhanced (100- to 500-fold) by various interfaces.	4-nitrophenyl acetate	55-76	pancreatic lipase	Homo sapiens	14-31	
2517482-1	1989	The activities of porcine pancreatic lipase (449 amino acid residues) toward two different substrates, p-nitrophenylacetate and tributyrylglycerol, and their dependence on histidine ethoxyformylation were studied.	4-nitrophenyl acetate	103-123	pancreatic lipase	Homo sapiens	26-43