PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
2760564-0	1989	Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N. Arginine carboxypeptidase activity in human serum, measured with the hippuryl-L-arginine substrate, is about three times higher than in human plasma.	hippuryl-L-arginine	157-176	carboxypeptidase N subunit 1	Homo sapiens	88-113
7559630-7	1995	Several active site-directed inhibitors also show generally similar potency toward the two enzymes, although guanidinoethylmercaptosuccinic acid is approximately 10-fold more potent, and hippuryl-Arg is approximately 100-fold more potent as an inhibitor of CPD than of CPE.	hippuryl-L-arginine	187-199	carboxypeptidase E	Bos taurus	269-272
8130654-2	1994	The trypsin-generated active form can not only cleave a small synthetic substrate, hippuryl-L-arginine, but can remove terminal arginine from bradykinin.	hippuryl-L-arginine	83-102	kininogen 1	Homo sapiens	142-152
1939207-10	1991	When activated by trypsin, it hydrolyzes carboxypeptidase B substrates, hippuryl-Arg and hippuryl-Lys, but not carboxypeptidase A substrates, and it is inhibited by the specific carboxypeptidase B inhibitor (DL-5-guanidinoethyl)mercaptosuccinic acid.	hippuryl-L-arginine	72-84	carboxypeptidase B1	Homo sapiens	178-196
3105932-1	1987	The enzyme sequentially converts creatine kinase MM3 to MM2 and MM1 and hydrolyzes lysine and arginine from hippuryl-L-lysine and hippuryl-L-arginine.	hippuryl-L-arginine	130-149	PNMA family member 2	Homo sapiens	56-59
3105932-1	1987	The enzyme sequentially converts creatine kinase MM3 to MM2 and MM1 and hydrolyzes lysine and arginine from hippuryl-L-lysine and hippuryl-L-arginine.	hippuryl-L-arginine	130-149	plexin B2	Homo sapiens	64-67
6644248-1	1983	Kininase I (carboxypeptidase N; EC 3.4.17.3) consists of carboxypeptidase N1 (CN1) and carboxypeptidase N2 (CN2); these two enzymes can be differentiated by their activities towards hippuryl-L-arginine and hippuryl-L-lysine, respectively.	hippuryl-L-arginine	182-201	carboxypeptidase N subunit 1	Homo sapiens	0-10
15802136-6	2005	The CPU activities measured using this kinetic assay were in the range of 97-103% of those determined with our HPLC-assisted reference assay, and the obtained K(m) and k(cat) values for hippuryl-l-arginine and bradykinin were in good accordance with those described in the literature.	hippuryl-L-arginine	186-205	carboxypeptidase B2	Homo sapiens	4-7
14190467-5	1964	Spectrophotometric studies of the hydrolysis of hippuryl-L-arginine confirmed the presence of a carboxypeptidase B-like activity in brain.	hippuryl-L-arginine	48-67	carboxypeptidase B1	Homo sapiens	96-114
7400116-3	1980	Several hydrophobic compounds acted as activators in dipeptide (Bz-Gly-L-Arg-OH, Z-Gly-L-Phe-OH) hydrolysis by bovine carboxypeptidase B.	hippuryl-L-arginine	64-79	carboxypeptidase B1	Bos taurus	118-136
180518-3	1976	The tumours under study also differed by the capacity to catalyze the splitting of hippuryl-L-arginine, synthetic substrate of carboxypeptidase B.	hippuryl-L-arginine	83-102	carboxypeptidase B1	Homo sapiens	127-145
16963025-3	2006	Experiments carried out on carboxypeptidase B in the absence of substrate and in the presence of saturating concentrations of hippuryl-Arg result in HDX kinetics that are indistinguishable.	hippuryl-L-arginine	126-138	carboxypeptidase B1	Homo sapiens	27-45
10351989-5	1999	The assay involved quantitative conversion of proCPU to active CPU by thrombin-thrombomodulin, a very efficient activator of proCPU, followed by determination of the enzymatic activity of CPU with the substrate hippuryl-L-arginine, using an HPLC-assisted determination of the released hippuric acid.	hippuryl-L-arginine	211-230	carboxypeptidase B2	Homo sapiens	49-52