PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8272161-7 1993 A prolonged interaction of active oxygen species with chemical carcinogens (N-nitroso- or diazonium compounds, PAH) can exhibit a significant promoting effect on the development of intestinal type of gastric cancer from its precancerous conditions, above all after partial gastrectomy. Oxygen 34-40 phenylalanine hydroxylase Homo sapiens 111-114 8921003-1 1996 Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme. Oxygen 119-127 phenylalanine hydroxylase Homo sapiens 10-35 8921003-1 1996 Mammalian phenylalanine hydroxylase (PAH) catalyses the conversion of L-phenylalanine to L-tyrosine in the presence of dioxygen and tetrahydrobiopterin; it is a highly regulated enzyme. Oxygen 119-127 phenylalanine hydroxylase Homo sapiens 37-40 35120400-7 2022 The hydrogel formulation exhibits a robust and validated visible red-orange-green "traffic light" spectrum in response to oxygen changes, regardless of swelling state, pH, or autofluorescence from skin, thereby enabling clinician friendly naked-eye feedback. Oxygen 122-128 phenylalanine hydroxylase Homo sapiens 168-170 34569192-0 2021 Construction of pH-Dependent Nanozymes with Oxygen Vacancies as the High-Efficient Reactive Oxygen Species Scavenger for Oral-Administrated Anti-Inflammatory Therapy. Oxygen 44-50 phenylalanine hydroxylase Homo sapiens 16-18 34679958-10 2021 This study demonstrated that the soil microbial community and availability of oxygen significantly affected the changes in moisture content, pH, and bacterial composition during the decomposition process. Oxygen 78-84 phenylalanine hydroxylase Homo sapiens 141-143 35535664-3 2022 It was found that a design concept with an oxygen-responsive dye in polymer nanoparticles and a pH-responsive dye in an organically modified siloxane polymer resulted in a robust pH/O2 dual optical sensor. Oxygen 43-49 phenylalanine hydroxylase Homo sapiens 179-181 35535664-3 2022 It was found that a design concept with an oxygen-responsive dye in polymer nanoparticles and a pH-responsive dye in an organically modified siloxane polymer resulted in a robust pH/O2 dual optical sensor. Oxygen 182-184 phenylalanine hydroxylase Homo sapiens 96-98 35535664-3 2022 It was found that a design concept with an oxygen-responsive dye in polymer nanoparticles and a pH-responsive dye in an organically modified siloxane polymer resulted in a robust pH/O2 dual optical sensor. Oxygen 182-184 phenylalanine hydroxylase Homo sapiens 179-181 34833408-5 2021 One of the earliest investigated local factors is the pH of wounds, studied in close relation to the local perfusion, oxygen tension, and lactate concentration. Oxygen 118-124 phenylalanine hydroxylase Homo sapiens 54-56 34622409-3 2021 The change in pH level affects the chemical oxygen demand (COD)/biochemical oxygen demand (BOD) ratio and when it is less than 0.63, chemical treatments are more effective over the biological treatment methods such as upflow anaerobic sludge blankets (UASB). Oxygen 44-50 phenylalanine hydroxylase Homo sapiens 14-16 34622409-3 2021 The change in pH level affects the chemical oxygen demand (COD)/biochemical oxygen demand (BOD) ratio and when it is less than 0.63, chemical treatments are more effective over the biological treatment methods such as upflow anaerobic sludge blankets (UASB). Oxygen 76-82 phenylalanine hydroxylase Homo sapiens 14-16 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. Oxygen 0-6 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. Oxygen 54-60 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. Oxygen 54-60 phenylalanine hydroxylase Homo sapiens 169-172 6495818-0 1984 Studies on the possible mechanism of inactivation of phenylalanine hydroxylase by destructive oxygen species. Oxygen 94-100 phenylalanine hydroxylase Homo sapiens 53-78 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. Oxygen 161-167 phenylalanine hydroxylase Homo sapiens 213-238 14031389-0 1962 The source of oxygen in the phenylalanine hydroxylase and the copamine-beta-hydroxylase catalyzed rections. Oxygen 14-20 phenylalanine hydroxylase Homo sapiens 28-53 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. Oxygen 12-18 phenylalanine hydroxylase Homo sapiens 34-59 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. Oxygen 12-18 phenylalanine hydroxylase Homo sapiens 61-64 33481326-0 2021 Delivering the Full Potential of Oxygen Evolving Electrocatalyst by Conditioning Electrolytes at Near-Neutral pH. Oxygen 33-39 phenylalanine hydroxylase Homo sapiens 110-112 33350421-0 2021 Defect-assisted electronic metal-support interactions: tuning the interplay between Ru nanoparticles and CuO supports for pH-neutral oxygen evolution. Oxygen 133-139 phenylalanine hydroxylase Homo sapiens 122-124 23480348-5 2013 Very importantly, the as-prepared PAH functionalized Pd icosahedra exhibit superior electrocatalytic activity and ethanol tolerant ability toward the oxygen reduction reaction (ORR) compared to the commercially available Pt black in alkaline media. Oxygen 150-156 phenylalanine hydroxylase Homo sapiens 34-37 33237716-0 2020 On the Origin of the Effect of pH in Oxygen Reduction Reaction for Nondoped and Edge-Type Quaternary N-Doped Metal-Free Carbon-Based Catalysts. Oxygen 37-43 phenylalanine hydroxylase Homo sapiens 31-33 33336311-5 2020 The aim of this review was to describe the pathophysiology and clinical consequences of arterial blood gases and pH after cardiac arrest.According to our findings, the optimal ventilator strategies in post cardiac arrest patients are not fully understood, and oxygen and carbon dioxide targets should take in consideration a complex pattern of pathophysiological factors. Oxygen 260-266 phenylalanine hydroxylase Homo sapiens 113-115 31789109-4 2019 Although a neglected clinical parameter, pH has implications for relatively all pathologies of wound healing affecting oxygen release, angiogenesis, protease activity, bacterial toxicity and antimicrobial activity. Oxygen 119-125 phenylalanine hydroxylase Homo sapiens 41-43 31038957-0 2019 Uncovered Dynamic Coupling Resolves the Ambiguous Mechanism of Phenylalanine Hydroxylase Oxygen Binding. Oxygen 89-95 phenylalanine hydroxylase Homo sapiens 63-88 31038957-3 2019 Despite intensive study, there is no consensus on the atomistic details of the mechanism of O2 binding and splitting by wild-type (WT) PAH and how it varies with PKU-inducing mutations, Arg158Gln and Glu280Lys. Oxygen 92-94 phenylalanine hydroxylase Homo sapiens 135-138 24713088-6 2014 In the PheH reaction, the transient formation of the 4a-hydroxypterin product was readily detected; tandem mass spectrometry confirmed attachment of the oxygen to C(4a). Oxygen 153-159 phenylalanine hydroxylase Homo sapiens 7-11 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. Oxygen 168-176 phenylalanine hydroxylase Homo sapiens 0-3 22616346-3 2011 Here we present a case of PCD with recurrent respiratory tract infections, bronchiectasis and severe PAH, who responded to treatment with Oxygen, IV broad spectrum antibiotics and oral sildenafil. Oxygen 138-144 phenylalanine hydroxylase Homo sapiens 101-104 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. Oxygen 139-145 phenylalanine hydroxylase Homo sapiens 0-25 15965718-0 2005 Dissolved oxygen saturation controls PAH biodegradation in freshwater estuary sediments. Oxygen 10-16 phenylalanine hydroxylase Homo sapiens 37-40 12744702-1 2003 Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate. Oxygen 154-162 phenylalanine hydroxylase Homo sapiens 0-25 12744702-1 2003 Phenylalanine hydroxylase (PAH) is a tetrahydrobiopterin-dependent enzyme that catalyzes the hydroxylation of L-phenylalanine (L-Phe) to L-tyrosine using dioxygen as an additional substrate. Oxygen 154-162 phenylalanine hydroxylase Homo sapiens 27-30 17443661-5 2007 The PAH enzyme converts phenylalanine to tyrosine in the presence of molecular oxygen and catalytic amounts of tetrahydrobiopterin (BH4), its nonprotein cofactor. Oxygen 79-85 phenylalanine hydroxylase Homo sapiens 4-7 15963939-3 2005 Using (6R)-tetrahydrobiopterin as electron donor in the phenylalanine hydroxylase (PAH) reaction, a stable stoichiometry of 1:1 was obtained between the amount of oxygen consumed and the tyrosine formation. Oxygen 163-169 phenylalanine hydroxylase Homo sapiens 56-81 15963939-3 2005 Using (6R)-tetrahydrobiopterin as electron donor in the phenylalanine hydroxylase (PAH) reaction, a stable stoichiometry of 1:1 was obtained between the amount of oxygen consumed and the tyrosine formation. Oxygen 163-169 phenylalanine hydroxylase Homo sapiens 83-86 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). Oxygen 180-188 phenylalanine hydroxylase Homo sapiens 77-102 12631267-6 2003 Despite favorable energy scores, tyrosine in a position trans to PAH residue His290 or TH residue His336 interferes with the access of the essential cofactor dioxygen to the catalytic center, thereby blocking the enzymatic reaction. Oxygen 158-166 phenylalanine hydroxylase Homo sapiens 65-68 12096915-4 2002 The enzyme phenylalanine hydroxylase (PheOH) catalyzes the hydroxylation of l-phenylalanine into l-tyrosine utilizing the cofactors (6R)-l-erythro-5,6,7,8 tetrahydrobiopterin (BH(4)) and molecular oxygen. Oxygen 197-203 phenylalanine hydroxylase Homo sapiens 11-36 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). Oxygen 180-188 phenylalanine hydroxylase Homo sapiens 104-107 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. Oxygen 141-147 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. Oxygen 141-147 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. Oxygen 112-118 phenylalanine hydroxylase Homo sapiens 50-75 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. Oxygen 13-20 phenylalanine hydroxylase Homo sapiens 84-109