PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18477464-1	2008	The iron atom in the nonheme iron monooxygenase phenylalanine hydroxylase is bound on one face by His285, His290, and Glu330.	Iron	4-8	phenylalanine hydroxylase	Rattus norvegicus	48-73	
8385134-3	1993	In contrast, recombinant enzyme expressed in Sf9 cells using a baculovirus vector was active and identical in several properties to phenylalanine hydroxylase from rat liver: the Km for 6-methyltetrahydropterin was 39 microM (compared with 35 microM for the rat liver enzyme), 1 atom of iron was "associated" per enzyme subunit, and electron paramagnetic resonance spectra showed that iron was distributed within two distinct environments.	Iron	286-290	phenylalanine hydroxylase	Rattus norvegicus	132-157	
8530485-2	1995	The non-heme iron-dependent metalloenzyme, rat hepatic phenylalanine hydroxylase (EC 1.14.16.1; phenylalanine 4-monooxygenase (PAH) was overexpressed in Escherichia coli and purified to homogeneity, allowing a detailed comparison of the kinetic, hydrodynamic, and spectroscopic properties of its allosteric states.	Iron	13-17	phenylalanine hydroxylase	Rattus norvegicus	55-80	
7929136-5	1994	BH4, 7,8-dihydrobiopterin (BH2), 6-methyltetrahydropterin, and 5-deaza-6-methyltetrahydropterin were found to bind to unactivated phenylalanine hydroxylase with a stoichiometry of 1/enzyme subunit and with hyperbolic kinetics; all appear to compete for the same binding site on the enzyme, and all appear to bind in the proximity of, but not to, the enzyme"s non-heme iron.	Iron	368-372	phenylalanine hydroxylase	Rattus norvegicus	130-155	
8385134-3	1993	In contrast, recombinant enzyme expressed in Sf9 cells using a baculovirus vector was active and identical in several properties to phenylalanine hydroxylase from rat liver: the Km for 6-methyltetrahydropterin was 39 microM (compared with 35 microM for the rat liver enzyme), 1 atom of iron was "associated" per enzyme subunit, and electron paramagnetic resonance spectra showed that iron was distributed within two distinct environments.	Iron	384-388	phenylalanine hydroxylase	Rattus norvegicus	132-157	
8385134-4	1993	Putative iron-binding sites of phenylalanine hydroxylase were studied by mutating either histidine 284 or 289 to serine and expressing these mutant enzymes (PAH-H284S and PAH-H289S) in Sf9 cells.	Iron	9-13	phenylalanine hydroxylase	Rattus norvegicus	31-56	
8385134-4	1993	Putative iron-binding sites of phenylalanine hydroxylase were studied by mutating either histidine 284 or 289 to serine and expressing these mutant enzymes (PAH-H284S and PAH-H289S) in Sf9 cells.	Iron	9-13	phenylalanine hydroxylase	Rattus norvegicus	157-160	
8385134-4	1993	Putative iron-binding sites of phenylalanine hydroxylase were studied by mutating either histidine 284 or 289 to serine and expressing these mutant enzymes (PAH-H284S and PAH-H289S) in Sf9 cells.	Iron	9-13	phenylalanine hydroxylase	Rattus norvegicus	171-174	
3356704-11	1988	The reaction of LOOH with phenylalanine hydroxylase strongly resembles the nonenzymatic reaction of LOOH with hematin, implying similar mechanisms for the two reactions and implicating the enzyme"s non-heme iron as both the site of reaction of LOOH and of electron transfer during oxidation and reduction.	Iron	207-211	phenylalanine hydroxylase	Rattus norvegicus	26-51	
7198642-0	1982	Iron-dependent regulation of rat liver phenylalanine hydroxylase activity in vivo, in vitro, and in perfused liver.	Iron	0-4	phenylalanine hydroxylase	Rattus norvegicus	39-64	
4854920-10	1974	The molecule of phenylalanine hydroxylase contained two atoms of iron, one atom of copper and one molecule of FAD; molybdenum was absent.	Iron	65-69	phenylalanine hydroxylase	Rattus norvegicus	16-41