PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7358628-4	1980	Aminopeptidase showed marked specificities for amino acid amides, such as L-leucineamide, L-phenylalanineamide, and L-methionineamide.	leucinamide	74-88	carboxypeptidase Q	Homo sapiens	0-14	
6435638-1	1983	Oxygen exchange in the amide group of leucine amide catalyzed by leucine aminopeptidase, and in leucyltyrosine amide catalyzed by porcine pepsin, was found to proceed mainly by the transfer of the leucyl residue onto the ammonia or tyrosine amide which are formed during the hydrolysis.	leucinamide	38-51	carboxypeptidase Q	Homo sapiens	73-87	
36029-7	1978	The aminopeptidase hydrolysed leucinamide and di- and tripeptides containing hydrophobic bulky amino acids as the N-terminal residue.	leucinamide	30-41	carboxypeptidase Q	Homo sapiens	4-18	
1116141-4	1975	The activity of aminopeptidase toward L-leucinamide and of arylamidase toward L-leucyl-beta-naphthylamide was higher in human stomach cancer tissue and lower in hepatic cancer tissue than in normal stomach and liver, respectively.	leucinamide	38-51	carboxypeptidase Q	Homo sapiens	16-30	
1116141-5	1975	In lung cancer tissue, the activity of aminopeptidase toward L-leucinamide was abnormally low, while the activity of arylamidase toward L-leucyl-beta-napthylamide was similar to that in normal lung.	leucinamide	61-74	carboxypeptidase Q	Homo sapiens	39-53