PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9188478-11	1997	This novel enzyme is capable of using the in vivo stable prodrugs, which are not substrates for the wild type hCPA1, as efficiently as the wild type hCPA1 uses its best substrates (i.e. MTX-alpha-phenylalanine).	methotrexate-alpha-phenylalanine	186-209	carboxypeptidase A1	Homo sapiens	110-115	
9188478-11	1997	This novel enzyme is capable of using the in vivo stable prodrugs, which are not substrates for the wild type hCPA1, as efficiently as the wild type hCPA1 uses its best substrates (i.e. MTX-alpha-phenylalanine).	methotrexate-alpha-phenylalanine	186-209	carboxypeptidase A1	Homo sapiens	149-154	
9188478-12	1997	Thus, the kcat/Km value for the wild type hCPA1 with MTX-alpha-phenylalanine is 0.44 microM-1 s-1, and kcat/Km values for hCPA1-T268G with MTX-alpha-3-cyclobutylphenylalanine and MTX-alpha-3-cyclopentyltyrosine are 1.8 and 0.16 microM-1 s-1, respectively.	methotrexate-alpha-phenylalanine	53-76	carboxypeptidase A1	Homo sapiens	42-47	
8806703-8	1996	The kcat/Km values for MTX-Phe were 440,000 and 90,000 M-1 s-1 for hCPA1 and hCPA2, respectively, and for MTX-naphthylAla these values were 1400 and 1,400,000 M-1 s-1 for hCPA1 and hCPA2, respectively.	methotrexate-alpha-phenylalanine	23-30	carboxypeptidase A1	Homo sapiens	67-72	
8806703-8	1996	The kcat/Km values for MTX-Phe were 440,000 and 90,000 M-1 s-1 for hCPA1 and hCPA2, respectively, and for MTX-naphthylAla these values were 1400 and 1,400,000 M-1 s-1 for hCPA1 and hCPA2, respectively.	methotrexate-alpha-phenylalanine	23-30	carboxypeptidase A1	Homo sapiens	171-176	
7834611-0	1995	Methotrexate-alpha-phenylalanine: optimization of methotrexate prodrug for activation by carboxypeptidase A-monoclonal antibody conjugate.	methotrexate-alpha-phenylalanine	0-32	carboxypeptidase A1	Homo sapiens	89-107	
7834611-2	1995	Production of MTX from MTX-Phe, catalyzed by bovine pancreas carboxypeptidase A (CPA), was 250-fold faster than the corresponding reaction involving methotrexate-alpha-alanine, previously the best MTX peptide substrate for the enzyme.	methotrexate-alpha-phenylalanine	23-30	carboxypeptidase A1	Homo sapiens	61-79	
7834611-2	1995	Production of MTX from MTX-Phe, catalyzed by bovine pancreas carboxypeptidase A (CPA), was 250-fold faster than the corresponding reaction involving methotrexate-alpha-alanine, previously the best MTX peptide substrate for the enzyme.	methotrexate-alpha-phenylalanine	23-30	carboxypeptidase A1	Homo sapiens	81-84	
7834611-3	1995	The amount of CPA required to make MTX-Phe equitoxic with MTX, when tested against UCLA-P3 human lung adenocarcinoma cells in vitro, was more than 10-fold lower than that required to achieve the same result with MTX-alpha-alanine.	methotrexate-alpha-phenylalanine	35-42	carboxypeptidase A1	Homo sapiens	14-17	
21559659-4	1994	MTX-Phe appeared to be the most suitable substrate for CP-A out of the eleven tested with a hydrolysis rate comparable to that of hippuryl-L-phenylalanine, a natural substrate for CP-A.	methotrexate-alpha-phenylalanine	0-7	carboxypeptidase A1	Homo sapiens	55-59	
21559659-4	1994	MTX-Phe appeared to be the most suitable substrate for CP-A out of the eleven tested with a hydrolysis rate comparable to that of hippuryl-L-phenylalanine, a natural substrate for CP-A.	methotrexate-alpha-phenylalanine	0-7	carboxypeptidase A1	Homo sapiens	180-184	
21559659-6	1994	These results suggest that MTX-Phe is a potent prodrug and could be used in a drug targeting model combining monoclonal antibodies coupled with CP-A for a more specific approach in cancer therapy.	methotrexate-alpha-phenylalanine	27-34	carboxypeptidase A1	Homo sapiens	144-148