PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10872454-1	1999	Phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase constitute a small family of monooxygenases that utilize tetrahydropterins as substrates.	tetrahydropterin	133-150	phenylalanine hydroxylase	Homo sapiens	0-75	
1944771-0	1991	Studies on the partially uncoupled oxidation of tetrahydropterins by phenylalanine hydroxylase.	tetrahydropterin	48-65	phenylalanine hydroxylase	Homo sapiens	69-94	
1944771-1	1991	The uncoupled portion of the partially uncoupled oxidation of tetrahydropterins by phenylalanine hydroxylase can be described by the same model as we have recently derived for the fully uncoupled reaction (Davis, M.D.	tetrahydropterin	62-79	phenylalanine hydroxylase	Homo sapiens	83-108	
1944771-7	1991	The 4a-carbinolamine tetrahydropterin intermediate has been observed during the fully uncoupled tyrosine-dependent oxidations of tetrahydropterin and 6-methyltetrahydropterin by lysolecithin-activated phenylalanine hydroxylase, suggesting that this species is also a common intermediate for uncoupled oxidations by this enzyme.	tetrahydropterin	21-37	phenylalanine hydroxylase	Homo sapiens	201-226	
3019383-5	1986	Oxygen consumption during PAH reduction by tetrahydropterin in the absence of phenylalanine but not in its presence explains the different reduction stoichiometries (tetrahydropterin:enzyme) that have been observed.	tetrahydropterin	43-59	phenylalanine hydroxylase	Homo sapiens	26-29	
2888478-3	1987	These results are in accord with shared mechanisms of oxygen activation by TH and the more commonly studied tetrahydropterin-dependent enzyme phenylalanine hydroxylase (PAH) and strongly suggest that a peroxytetrahydropterin is the hydroxylating species generated during TH turnover.	tetrahydropterin	108-124	phenylalanine hydroxylase	Homo sapiens	142-167	
2888478-3	1987	These results are in accord with shared mechanisms of oxygen activation by TH and the more commonly studied tetrahydropterin-dependent enzyme phenylalanine hydroxylase (PAH) and strongly suggest that a peroxytetrahydropterin is the hydroxylating species generated during TH turnover.	tetrahydropterin	108-124	phenylalanine hydroxylase	Homo sapiens	169-172	
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	tetrahydropterin	172-188	phenylalanine hydroxylase	Homo sapiens	34-59	
6495818-6	1984	These findings suggest that the termination of phenylalanine hydroxylation in the absence of hydrogen peroxide removing reactions is probably due to destructive oxygen species generated at the active site iron of phenylalanine hydroxylase in the presence of H2O2 and the tetrahydropterin cofactor.	tetrahydropterin	271-287	phenylalanine hydroxylase	Homo sapiens	213-238	
4084494-0	1985	Mechanism of "uncoupled" tetrahydropterin oxidation by phenylalanine hydroxylase.	tetrahydropterin	23-41	phenylalanine hydroxylase	Homo sapiens	55-80	
4084494-1	1985	Phenylalanine hydroxylase can catalyze the oxidation of its tetrahydropterin cofactor without concomitant substrate hydroxylation.	tetrahydropterin	60-76	phenylalanine hydroxylase	Homo sapiens	0-25	
4084494-8	1985	A mechanism is proposed for the uncoupled oxidation of tetrahydropterins by phenylalanine hydroxylase, and the significance of these findings is discussed.	tetrahydropterin	55-72	phenylalanine hydroxylase	Homo sapiens	76-101	
7096201-7	1982	It inhibited phenylalanine hydroxylase by 50% at a concentration of 1.8 x 10(-5) M. This inhibition was a mixed type with either a tetrahydropterin cofactor, DMPH4, or with the substrate phenylalanine, which was different from the inhibition by oudenone.	tetrahydropterin	131-147	phenylalanine hydroxylase	Homo sapiens	13-38	
6282659-1	1982	The site of oxygen binding during phenylalanine hydroxylase (PAH)-catalyzed turnover of phenylalanine to tyrosine has been tentatively identified as the 4a position of the tetrahydropterin cofactor, based on the spectral characteristics of an intermediate generated from both 6-methyltetrahydropterin and tetrahydrobiopterin during turnover.	tetrahydropterin	172-188	phenylalanine hydroxylase	Homo sapiens	61-64	
19281164-1	2009	The nonheme iron enzyme phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase catalyze the hydroxylation of their aromatic amino acid substrates using a tetrahydropterin as the source of electrons.	tetrahydropterin	175-191	phenylalanine hydroxylase	Homo sapiens	24-49	
15493924-0	2004	Thermodynamic characterization of the binding of tetrahydropterins to phenylalanine hydroxylase.	tetrahydropterin	49-66	phenylalanine hydroxylase	Homo sapiens	70-95