PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 27940234-2 2017 Specifically, we prepared iron doped polyacrylic hydrazide modified reduced graphene nanocomposites (Fe@RGO/PAH) by in-situ polymerization approach and subsequent a one-pot reaction with hydrazine. Iron 26-30 phenylalanine hydroxylase Homo sapiens 108-111 27940234-3 2017 The resulting Fe@RGO/PAH nanocomposites displayed low nonspecific adsorption to analytes (11% quenching caused by nonspecific adsorption) due to electrostatic, energetic and steric effect of the nanocomposites. Iron 14-16 phenylalanine hydroxylase Homo sapiens 21-24 23860686-1 2013 Phenylalanine hydroxylase (PAH) is a non-heme iron enzyme that catalyzes oxidation of phenylalanine to tyrosine, a reaction that must be kept under tight regulatory control. Iron 46-50 phenylalanine hydroxylase Homo sapiens 0-25 23860686-1 2013 Phenylalanine hydroxylase (PAH) is a non-heme iron enzyme that catalyzes oxidation of phenylalanine to tyrosine, a reaction that must be kept under tight regulatory control. Iron 46-50 phenylalanine hydroxylase Homo sapiens 27-30 16676991-0 2006 EPR and UV-vis studies of the nitric oxide adducts of bacterial phenylalanine hydroxylase: effects of cofactor and substrate on the iron environment. Iron 132-136 phenylalanine hydroxylase Homo sapiens 64-89 23425894-0 2013 Health implications of PAH release from coated cast iron drinking water distribution systems in The Netherlands. Iron 52-56 phenylalanine hydroxylase Homo sapiens 23-26 19123805-5 2009 Films constituted by more than nine PSS/PAH bilayers are still permeable to hexacyanoferrate(II) ions, Fe(CN)(6)4-, whatever the nature of the supporting salt anion. Iron 103-105 phenylalanine hydroxylase Homo sapiens 40-43 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. Iron 12-16 phenylalanine hydroxylase Homo sapiens 24-49 23045014-2 2009 PAH is a non-heme-iron-dependent protein that normally catalyzes the C-oxidation of phenylalanine (Phe) to tyrosine (Tyr) in the presence of BH(4), utilizing molecular dioxygen as an additional substrate. Iron 18-22 phenylalanine hydroxylase Homo sapiens 0-3 16935936-6 2006 The molecular dynamics simulated structures of the pterin-PAH complexes indicate that 7(S)BH4 inhibition is due to its interaction with the polar region at the pterin binding site close to Ser-251, whereas its low efficiency as cofactor is related to a suboptimal positioning toward the catalytic iron. Iron 297-301 phenylalanine hydroxylase Homo sapiens 58-61 15917086-0 2005 The active site residue tyrosine 325 influences iron binding and coupling efficiency in human phenylalanine hydroxylase. Iron 48-52 phenylalanine hydroxylase Homo sapiens 94-119 15917086-13 2005 On the other hand, compared to wild-type PAH, Y325L shows reduced specific activity, decreased coupling efficiency and decreased iron content. Iron 129-133 phenylalanine hydroxylase Homo sapiens 41-44 15917086-16 2005 Tyr325 thus appears to have an important role ensuring stoichiometric binding of iron, correct geometry of the complexes with substrate and cofactor and, consequently, a right coupling efficiency of the PAH reaction. Iron 81-85 phenylalanine hydroxylase Homo sapiens 203-206 12733906-1 2003 Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism. Iron 76-80 phenylalanine hydroxylase Homo sapiens 0-25 12733906-1 2003 Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent, nonheme iron enzyme that catalyzes the hydroxylation of L-Phe to L-Tyr in the rate-limiting step of phenylalanine catabolism. Iron 76-80 phenylalanine hydroxylase Homo sapiens 27-30 12696880-0 2003 Posttranslational hydroxylation of human phenylalanine hydroxylase is a novel example of enzyme self-repair within the second coordination sphere of catalytic iron. Iron 159-163 phenylalanine hydroxylase Homo sapiens 41-66 12696880-1 2003 Phenylalanine hydroxylase, a mononuclear non-heme iron enzyme, catalyzes the hydroxylation of phenylalanine to tyrosine in the presence of oxygen and reduced pterin cofactor. Iron 50-54 phenylalanine hydroxylase Homo sapiens 0-25 12696880-3 2003 One such interaction involves Tyr325 in human phenylalanine hydroxylase (hPAH), which forms a hydrogen-bonding network with an aqua ligand on iron and the pterin cofactor. Iron 142-146 phenylalanine hydroxylase Homo sapiens 46-71 12696880-3 2003 One such interaction involves Tyr325 in human phenylalanine hydroxylase (hPAH), which forms a hydrogen-bonding network with an aqua ligand on iron and the pterin cofactor. Iron 142-146 phenylalanine hydroxylase Homo sapiens 73-77 11472242-3 2001 TPH belongs to the family of the aromatic amino acid hydroxylases, including phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH), which all have a strict requirement for dioxygen, non-heme iron (II) and tetrahydrobiopterin (BH4). Iron 199-203 phenylalanine hydroxylase Homo sapiens 77-102 12631267-8 2003 Two alternative conformations, rotated 180 degrees around an imaginary iron-catecholamine axis, were found for DA and l-DOPA in PAH and for DA in TH. Iron 71-75 phenylalanine hydroxylase Homo sapiens 128-131 11472242-3 2001 TPH belongs to the family of the aromatic amino acid hydroxylases, including phenylalanine hydroxylase (PAH) and tyrosine hydroxylase (TH), which all have a strict requirement for dioxygen, non-heme iron (II) and tetrahydrobiopterin (BH4). Iron 199-203 phenylalanine hydroxylase Homo sapiens 104-107 11301319-0 2001 The effect of substrate, dihydrobiopterin, and dopamine on the EPR spectroscopic properties and the midpoint potential of the catalytic iron in recombinant human phenylalanine hydroxylase. Iron 136-140 phenylalanine hydroxylase Homo sapiens 162-187 11301319-1 2001 Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr. Iron 78-82 phenylalanine hydroxylase Homo sapiens 0-25 11301319-1 2001 Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin (BH(4)) and non-heme iron-dependent enzyme that hydroxylates L-Phe to L-Tyr. Iron 78-82 phenylalanine hydroxylase Homo sapiens 27-30 9819237-1 1998 The aromatic amino acid hydroxylases tyrosine and phenylalanine hydroxylase both contain non-heme iron, utilize oxygen and tetrahydrobiopterin, and are tetramers of identical subunits. Iron 98-102 phenylalanine hydroxylase Homo sapiens 50-75 10037716-0 1999 The accessibility of iron at the active site of recombinant human phenylalanine hydroxylase to water as studied by 1H NMR paramagnetic relaxation. Iron 21-25 phenylalanine hydroxylase Homo sapiens 66-91 10037716-7 1999 Thus, the recombinant human PAH appears to have a more solvent-accessible catalytic iron than the rat enzyme, in which the water coordinated to the metal is slowly exchanging with the solvent. Iron 84-88 phenylalanine hydroxylase Homo sapiens 28-31 10875932-8 2000 In conclusion, serine 349, located in the three-dimensional structure lining the active site and involved in the structural maintenance of the iron binding site, is essential for the structural stability and assembly and also for the catalytic properties of the PAH enzyme, whereas the L348V and V388M mutations affect the folding properties and stability of the protein. Iron 143-147 phenylalanine hydroxylase Homo sapiens 262-265 10610798-1 1999 Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate. Iron 70-74 phenylalanine hydroxylase Homo sapiens 0-25 10610798-1 1999 Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin and non-heme iron-dependent enzyme that hydroxylates L-Phe to l-Tyr using molecular oxygen as additional substrate. Iron 70-74 phenylalanine hydroxylase Homo sapiens 27-30 10610798-3 1999 The conformation and distances to the catalytic iron of both L-Phe and the cofactor analogue L-erythro-7,8-dihydrobiopterin (BH2) simultaneously bound to recombinant human PAH have been estimated by (1)H NMR. Iron 48-52 phenylalanine hydroxylase Homo sapiens 172-175 10610798-6 1999 The mode of coordination of Glu330 to the iron moiety seems to determine the amino acid substrate specificity in PAH and in the homologous enzyme tyrosine hydroxylase. Iron 42-46 phenylalanine hydroxylase Homo sapiens 113-116 9819237-3 1998 The hydroxyl oxygens of tyrosine 371 in tyrosine hydroxylase and of tyrosine 325 of phenylalanine hydroxylase are 5 and 4.5 A, respectively, away from the active site iron in the enzymes. Iron 167-171 phenylalanine hydroxylase Homo sapiens 84-109 8425536-2 1993 The effect of the paramagnetic high-spin Fe(III) ion in phenylalanine 4-monooxygenase (phenylalanine hydroxylase, EC 1.14.16.1) on the water proton longitudinal relaxation rate has been used to study the environment of the iron center. Iron 207-211 phenylalanine hydroxylase Homo sapiens 56-85 9109411-1 1997 A recombinant truncated form (delta1-102/delta428-452) of the non-heme iron-dependent metalloenzyme human phenylalanine hydroxylase (hPAH, phenylalanine 4-monooxygenase; EC 1.14.16.1) was expressed in E. coli, purified to homogeneity as a homodimer (70 kDa) and crystallized using the hanging drop vapour diffusion method. Iron 71-75 phenylalanine hydroxylase Homo sapiens 106-131 9109411-1 1997 A recombinant truncated form (delta1-102/delta428-452) of the non-heme iron-dependent metalloenzyme human phenylalanine hydroxylase (hPAH, phenylalanine 4-monooxygenase; EC 1.14.16.1) was expressed in E. coli, purified to homogeneity as a homodimer (70 kDa) and crystallized using the hanging drop vapour diffusion method. Iron 71-75 phenylalanine hydroxylase Homo sapiens 139-168 8108417-4 1994 The P. aeruginosa PhhA appears to contain iron and is pterin dependent. Iron 42-46 phenylalanine hydroxylase Homo sapiens 18-22 8425536-2 1993 The effect of the paramagnetic high-spin Fe(III) ion in phenylalanine 4-monooxygenase (phenylalanine hydroxylase, EC 1.14.16.1) on the water proton longitudinal relaxation rate has been used to study the environment of the iron center. Iron 207-211 phenylalanine hydroxylase Homo sapiens 87-112 34461510-5 2022 A favourable reduction of pH and a betterment of parameters related to colour were detected in wines from iron deficient subzones. Iron 106-110 phenylalanine hydroxylase Homo sapiens 26-28 34857271-0 2021 Mg-Fe layered double hydroxides modified titanium enhanced the adhesion of human gingival fibroblasts through regulation of local pH level. Iron 3-5 phenylalanine hydroxylase Homo sapiens 130-132 34928835-5 2021 The kinetics study revealed that equilibrium was reached after 120 min for both metals, and maximal adsorbed quantities of cadmium (76 mg/g) and iron (55 mg/g ) were obtained at pH = 10 and 8 respectively. Iron 145-149 phenylalanine hydroxylase Homo sapiens 178-180 34212661-7 2021 In addition, pH exhibited a significant negative correlation with Fe and Fe nanoparticles. Iron 66-68 phenylalanine hydroxylase Homo sapiens 13-15 34361737-4 2021 Indeed, the precipitation of Fe(III) at pH > 4 interferes with the recycling of Fe species and inhibits oxidation in homogeneous Fenton; in contrast, suspended ZVI as iron source is less sensitive to the increase of pH. Iron 80-82 phenylalanine hydroxylase Homo sapiens 40-42 34361737-4 2021 Indeed, the precipitation of Fe(III) at pH > 4 interferes with the recycling of Fe species and inhibits oxidation in homogeneous Fenton; in contrast, suspended ZVI as iron source is less sensitive to the increase of pH. Iron 80-82 phenylalanine hydroxylase Homo sapiens 216-218 34361737-4 2021 Indeed, the precipitation of Fe(III) at pH > 4 interferes with the recycling of Fe species and inhibits oxidation in homogeneous Fenton; in contrast, suspended ZVI as iron source is less sensitive to the increase of pH. Iron 167-171 phenylalanine hydroxylase Homo sapiens 216-218 34212661-7 2021 In addition, pH exhibited a significant negative correlation with Fe and Fe nanoparticles. Iron 73-75 phenylalanine hydroxylase Homo sapiens 13-15 6282659-4 1982 PAH also requires 1.0 iron per 50,000-dalton subunit for maximal activity. Iron 22-26 phenylalanine hydroxylase Homo sapiens 0-3 3772017-3 1986 The method has been used to determine the stoichiometry of iron for nanomole quantities of heme-iron proteins, iron-sulfur proteins, complex iron-sulfur proteins, as well as in phenylalanine hydroxylase, an enzyme with iron in an undetermined coordination. Iron 59-63 phenylalanine hydroxylase Homo sapiens 177-202 3019383-1 1986 Iron can be bound to phenylalanine hydroxylase (PAH) in two environments. Iron 0-4 phenylalanine hydroxylase Homo sapiens 21-46 3019383-1 1986 Iron can be bound to phenylalanine hydroxylase (PAH) in two environments. Iron 0-4 phenylalanine hydroxylase Homo sapiens 48-51 3026504-1 1987 Lineshape simulations are presented for the multiple, overlapping X-band electron paramagnetic resonance (EPR) spectra in two non-heme, high-spin iron proteins: phenylalanine hydroxylase (PAH) and diferric transferrin. Iron 146-150 phenylalanine hydroxylase Homo sapiens 161-186 3026504-1 1987 Lineshape simulations are presented for the multiple, overlapping X-band electron paramagnetic resonance (EPR) spectra in two non-heme, high-spin iron proteins: phenylalanine hydroxylase (PAH) and diferric transferrin. Iron 146-150 phenylalanine hydroxylase Homo sapiens 188-191 3026504-4 1987 In both PAH and transferrin, at least one of the iron sites is characterized by the ratio of zero-field splitting parameters, E/D, near 1/3 and a broad, asymmetric lineshape. Iron 49-53 phenylalanine hydroxylase Homo sapiens 8-11 3026504-9 1987 When applied to spectra of PAH in the resting state, the E/D-distribution approach accounts for the intensity of one of the two major species of iron. Iron 145-149 phenylalanine hydroxylase Homo sapiens 27-30 6324864-0 1984 Reductive activation of phenylalanine hydroxylase and its effect on the redox state of the non-heme iron. Iron 100-104 phenylalanine hydroxylase Homo sapiens 24-49 7054185-2 1982 Phenylalanine hydroxylase requires 1.0 mol of iron/Mr = 50,000 subunit for maximal activity. Iron 46-50 phenylalanine hydroxylase Homo sapiens 0-25 4854919-10 1974 Iron-chelating and copper-chelating agents inhibited human phenylalanine hydroxylase. Iron 0-4 phenylalanine hydroxylase Homo sapiens 59-84 33934496-3 2021 This study examines impacts of pH and the supply of acetate, sulfate, and goethite on the ratio of iron to sulfate reduction in semi-continuous sediment bioreactors. Iron 99-103 phenylalanine hydroxylase Homo sapiens 31-33 33934496-5 2021 Results show that pH had a greater influence than acetate supply on the ratio of iron to sulfate reduction, and that the impact of acetate supply on the ratio depended on pH. Iron 81-85 phenylalanine hydroxylase Homo sapiens 18-20 33934496-6 2021 In acidic reactors (pH 6.0 media), the ratio of iron to sulfate reduction decreased from 3:1 to 2:1 as acetate supply increased (0-1 mM). Iron 48-52 phenylalanine hydroxylase Homo sapiens 20-22 33934496-9 2021 Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases. Iron 41-45 phenylalanine hydroxylase Homo sapiens 80-82 33934496-9 2021 Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases. Iron 41-45 phenylalanine hydroxylase Homo sapiens 161-163 33934496-9 2021 Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases. Iron 101-105 phenylalanine hydroxylase Homo sapiens 80-82 33934496-9 2021 Thus, the influence of sulfate supply on iron reduction extent also depended on pH and suggests that iron reduction grows more dependent on sulfate reduction as pH increases. Iron 101-105 phenylalanine hydroxylase Homo sapiens 161-163 33934496-10 2021 Our results compare well to trends in groundwater geochemistry and provide further evidence that pH is a major control on iron and sulfate reduction in systems with crystalline (oxyhydr)oxides. Iron 122-126 phenylalanine hydroxylase Homo sapiens 97-99 32957294-3 2020 In the system of iron-carbon internal electrolysis coupled with persulfate, the iron-carbon internal electrolysis and persulfate had a significant mutual influence, exhibiting a wide range of pH in the treatment process. Iron 17-21 phenylalanine hydroxylase Homo sapiens 192-194 33934496-0 2021 Influences of pH and substrate supply on the ratio of iron to sulfate reduction. Iron 54-58 phenylalanine hydroxylase Homo sapiens 14-16 32957294-3 2020 In the system of iron-carbon internal electrolysis coupled with persulfate, the iron-carbon internal electrolysis and persulfate had a significant mutual influence, exhibiting a wide range of pH in the treatment process. Iron 80-84 phenylalanine hydroxylase Homo sapiens 192-194 31038957-1 2019 Phenylalanine hydroxylase (PAH) is an iron enzyme catalyzing the oxidation of l-Phe to l-Tyr during phenylalanine catabolism. Iron 38-42 phenylalanine hydroxylase Homo sapiens 0-25 31038957-1 2019 Phenylalanine hydroxylase (PAH) is an iron enzyme catalyzing the oxidation of l-Phe to l-Tyr during phenylalanine catabolism. Iron 38-42 phenylalanine hydroxylase Homo sapiens 27-30 29101890-8 2018 The sudden increase in atmospheric PAH concentrations in the winter of 2014 may also be due to iron manufacturing. Iron 95-99 phenylalanine hydroxylase Homo sapiens 35-38