PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 9542220-4 1998 In the second pregnancy, an experimental hyperphenylalaninemia was provoked by means of injection of phenylalanine and chlorophenylalanine (phenylalanine-hydroxylase inhibitor). Phenylalanine 46-59 phenylalanine hydroxylase Rattus norvegicus 140-165 15764292-4 2004 Urinary and plasma phenylacetylglycine (PAG) and hepatic portal:aortal phenylacetate (PA) ratio were increased, whereas hepatic phenylalanine hydroxylase (PAH) activity and plasma phenylalanine:tyrosine ratio were not affected. Phenylalanine 128-141 phenylalanine hydroxylase Rattus norvegicus 155-158 12668065-1 2003 Phenylketonuria (PKU) is a disorder characterized by an interruption in the conversion of phenylalanine to tyrosine, a reaction catalyzed by phenylalanine hydroxylase (PAH). Phenylalanine 90-103 phenylalanine hydroxylase Rattus norvegicus 141-166 16139311-2 2006 This study investigated the relationship between the PheBT parameter 13C excretion rate constant (PheBT-k) and activity of the phenylalanine metabolic rate-limiting enzyme phenylalanine hydroxylase (PAH) in rat liver. Phenylalanine 127-140 phenylalanine hydroxylase Rattus norvegicus 172-197 16429477-3 2006 This study investigated the relationship between the parameters of PheBT, performed with air isotope ratio mass spectrometry, and the activity of phenylalanine hydroxylase (PAH), the phenylalanine metabolism rate-limiting enzyme, in rat liver, and proposes valid parameters for the assessment of liver function. Phenylalanine 146-159 phenylalanine hydroxylase Rattus norvegicus 173-176 11410294-1 2001 Phenylalanine hydroxylase (PAH, EC 1.14.16.1) is a highly regulated liver enzyme which catalyses the conversion of L-phenylalanine to L-tyrosine, the rate-limiting step in the catabolic pathway of this amino acid. Phenylalanine 115-130 phenylalanine hydroxylase Rattus norvegicus 0-25 10197570-1 1999 BACKGROUND: Branched-chain amino acids have been reported to improve fetal brain development in a rat model in which maternal phenylketonuria (PKU) is induced by the inclusion of an inhibitor of phenylalanine hydroxylase, DL-p-chlorophenylalanine, and L-phenylalanine in the diet. Phenylalanine 252-267 phenylalanine hydroxylase Rattus norvegicus 195-220 9012811-0 1997 The role of phenylalanine in structure-function relationships of phenylalanine hydroxylase revealed by radiation target analysis. Phenylalanine 12-25 phenylalanine hydroxylase Rattus norvegicus 65-90 1350256-2 1992 A 4a-carbinolamine intermediate is generated stoichiometrically during the tetrahydrobiopterin-dependent phenylalanine hydroxylation reaction catalyzed by phenylalanine hydroxylase. Phenylalanine 105-118 phenylalanine hydroxylase Rattus norvegicus 155-180 7846072-3 1995 Bound BH4 appears bound to PAH; the PAH-BH4 complex has much less catalytic activity and is less readily phenylalanine activated than uncomplexed enzyme. Phenylalanine 105-118 phenylalanine hydroxylase Rattus norvegicus 36-39 7846072-7 1995 The data provide support in vivo that phenylalanine and BH4 are positive and negative regulators of the activity and activation state of PAH in the proposed manner; they also imply that regulation of BH4 turnover and PAH activity are linked processes, which are both controlled by phenylalanine concentration. Phenylalanine 38-51 phenylalanine hydroxylase Rattus norvegicus 137-140 7846072-7 1995 The data provide support in vivo that phenylalanine and BH4 are positive and negative regulators of the activity and activation state of PAH in the proposed manner; they also imply that regulation of BH4 turnover and PAH activity are linked processes, which are both controlled by phenylalanine concentration. Phenylalanine 38-51 phenylalanine hydroxylase Rattus norvegicus 217-220 7846072-7 1995 The data provide support in vivo that phenylalanine and BH4 are positive and negative regulators of the activity and activation state of PAH in the proposed manner; they also imply that regulation of BH4 turnover and PAH activity are linked processes, which are both controlled by phenylalanine concentration. Phenylalanine 281-294 phenylalanine hydroxylase Rattus norvegicus 137-140 7846072-7 1995 The data provide support in vivo that phenylalanine and BH4 are positive and negative regulators of the activity and activation state of PAH in the proposed manner; they also imply that regulation of BH4 turnover and PAH activity are linked processes, which are both controlled by phenylalanine concentration. Phenylalanine 281-294 phenylalanine hydroxylase Rattus norvegicus 217-220 1316838-6 1992 Phenylalanine was a negative modulator of the phosphorylation of phenylalanine hydroxylase induced by incubating cells with vasopressin or with the phosphatase inhibitor okadaic acid. Phenylalanine 0-13 phenylalanine hydroxylase Rattus norvegicus 65-90 8925406-1 1996 Phenylalanine hydroxylase catalyzes the major regulatory step of the phenylalanine degradation pathway. Phenylalanine 69-82 phenylalanine hydroxylase Rattus norvegicus 0-25 7846072-1 1995 This work had two purposes: (i) to determine in vivo whether liver phenylalanine hydroxylase (PAH) is regulated by its substrates phenylalanine and tetrahydrobiopterin (BH4) as studies with purified enzyme suggest and (ii) to investigate in vivo the relationship between PAH activity and BH4 turnover. Phenylalanine 67-80 phenylalanine hydroxylase Rattus norvegicus 94-97 7929136-3 1994 Activation by phenylalanine and reduction by the co-factor (6R)-tetrahydrobiopterin (BH4) are required for formation of active liver phenylalanine hydroxylase. Phenylalanine 14-27 phenylalanine hydroxylase Rattus norvegicus 133-158 7929136-7 1994 The pterin- and phenylalanine-binding sites on activated phenylalanine hydroxylase appear to be part of the enzyme"s active site. Phenylalanine 16-29 phenylalanine hydroxylase Rattus norvegicus 57-82 7929137-3 1994 Effects of phenylalanine and di- and tetrahydropterins on presteady-state and steady-state catalytic behavior of rat liver phenylalanine hydroxylase are analyzed. Phenylalanine 11-24 phenylalanine hydroxylase Rattus norvegicus 123-148 7929137-14 1994 Using kinetic constants measured in this and earlier work, quantitative effects of phenylalanine and BH4 regulation on the rate of the phenylalanine hydroxylase reaction in vitro and in vivo are calculated. Phenylalanine 83-96 phenylalanine hydroxylase Rattus norvegicus 135-160 7904815-1 1994 The conversion of phenylalanine to tyrosine is accelerated approximately five fold by phosphorylation of the enzyme which catalyzes this step, phenylalanine hydroxylase. Phenylalanine 18-31 phenylalanine hydroxylase Rattus norvegicus 143-168 8323303-1 1993 Phenylalanine hydroxylase, a tetrahydrobiopterin (BH4)-dependent oxygenase, catalyzes the conversion of phenylalanine to tyrosine. Phenylalanine 104-117 phenylalanine hydroxylase Rattus norvegicus 0-25 1730677-0 1992 Phenylalanine-induced phosphorylation and activation of rat hepatic phenylalanine hydroxylase in vivo. Phenylalanine 0-13 phenylalanine hydroxylase Rattus norvegicus 68-93 1422220-1 1992 Phenylalanine hydroxylase, important in phenylalanine metabolism in mammals, is regulated through short-term (activation) and long-term (induction) mechanisms. Phenylalanine 40-53 phenylalanine hydroxylase Rattus norvegicus 0-25 1730677-8 1992 However, we show for the first time in the present study that in vivo treatment with phenylalanine alone results in a 4-fold increase in the BH4-dependent activity of phenylalanine hydroxylase concomitant with a significant incorporation of phosphate into phenylalanine hydroxylase (0.51 mol of 32Pi/mol of hydroxylase subunit). Phenylalanine 85-98 phenylalanine hydroxylase Rattus norvegicus 167-192 1730677-8 1992 However, we show for the first time in the present study that in vivo treatment with phenylalanine alone results in a 4-fold increase in the BH4-dependent activity of phenylalanine hydroxylase concomitant with a significant incorporation of phosphate into phenylalanine hydroxylase (0.51 mol of 32Pi/mol of hydroxylase subunit). Phenylalanine 85-98 phenylalanine hydroxylase Rattus norvegicus 256-281 1730677-11 1992 A model is, thereby, proposed with respect to the ligand binding effects of phenylalanine on the state of phosphorylation and activation of phenylalanine hydroxylase. Phenylalanine 76-89 phenylalanine hydroxylase Rattus norvegicus 140-165 2065060-12 1991 Labeling of the enzyme resulted in 1 mol of fluorescein bound per phenylalanine hydroxylase subunit and a concomitant activation of phenylalanine hydroxylase to 82% of the activity found with phenylalanine-activated enzyme. Phenylalanine 66-79 phenylalanine hydroxylase Rattus norvegicus 132-157 2722790-1 1989 In the presence of phenylalanine and molecular oxygen, activated phenylalanine hydroxylase catalyzes the oxidation of tetrahydrobiopterin. Phenylalanine 19-32 phenylalanine hydroxylase Rattus norvegicus 65-90 2365689-0 1990 Mechanism of phenylalanine regulation of phenylalanine hydroxylase. Phenylalanine 13-26 phenylalanine hydroxylase Rattus norvegicus 41-66 2365689-1 1990 The mechanism of phenylalanine regulation of rat liver phenylalanine hydroxylase was studied. Phenylalanine 17-30 phenylalanine hydroxylase Rattus norvegicus 55-80 2365689-2 1990 We show that phenylalanine "activates" phenylalanine hydroxylase, converting it from an inactive to active form, by binding at a true allosteric regulatory site. Phenylalanine 13-26 phenylalanine hydroxylase Rattus norvegicus 39-64 3408719-1 1988 The phenylalanine analogue L-[2,5-H2]phenylalanine (1) was found to be a viable substrate (KM = 0.45 mM, kcat = 8 s-1) for L-phenylalanine-activated, rat liver phenylalanine hydroxylase (EC 1.14.16.1) (PAH). Phenylalanine 4-17 phenylalanine hydroxylase Rattus norvegicus 202-205 3408719-1 1988 The phenylalanine analogue L-[2,5-H2]phenylalanine (1) was found to be a viable substrate (KM = 0.45 mM, kcat = 8 s-1) for L-phenylalanine-activated, rat liver phenylalanine hydroxylase (EC 1.14.16.1) (PAH). Phenylalanine 4-17 phenylalanine hydroxylase Rattus norvegicus 160-185 2930457-1 1989 Phenylalanine hydroxylase purified from rat liver shows positive co-operativity in response to variations in phenylalanine concentration when assayed with the naturally occurring cofactor tetrahydrobiopterin. Phenylalanine 109-122 phenylalanine hydroxylase Rattus norvegicus 0-25 3408719-1 1988 The phenylalanine analogue L-[2,5-H2]phenylalanine (1) was found to be a viable substrate (KM = 0.45 mM, kcat = 8 s-1) for L-phenylalanine-activated, rat liver phenylalanine hydroxylase (EC 1.14.16.1) (PAH). Phenylalanine 123-138 phenylalanine hydroxylase Rattus norvegicus 160-185 3408719-1 1988 The phenylalanine analogue L-[2,5-H2]phenylalanine (1) was found to be a viable substrate (KM = 0.45 mM, kcat = 8 s-1) for L-phenylalanine-activated, rat liver phenylalanine hydroxylase (EC 1.14.16.1) (PAH). Phenylalanine 123-138 phenylalanine hydroxylase Rattus norvegicus 202-205 3408719-4 1988 The enzymatic epoxidation of 1 is consistent with the hypothesis of an intermediate arene oxide on the reaction coordinate for PAH hydroxylation of L-phenylalanine. Phenylalanine 148-163 phenylalanine hydroxylase Rattus norvegicus 127-130 3356704-9 1988 Phenylalanine hydroxylase is an excellent catalyst for this reaction: the turnover number with LOOH is slightly greater than with phenylalanine; the Km(app) for LOOH is 11 +/- 4 microM; and the kcat/Km ratio for LOOH is about 25 times greater than for phenylalanine. Phenylalanine 130-143 phenylalanine hydroxylase Rattus norvegicus 0-25 3356704-9 1988 Phenylalanine hydroxylase is an excellent catalyst for this reaction: the turnover number with LOOH is slightly greater than with phenylalanine; the Km(app) for LOOH is 11 +/- 4 microM; and the kcat/Km ratio for LOOH is about 25 times greater than for phenylalanine. Phenylalanine 252-265 phenylalanine hydroxylase Rattus norvegicus 0-25 3356704-10 1988 LOOH and phenylalanine appear to react at different sites on phenylalanine appear to react at different sites on phenylalanine hydroxylase, and the reaction of LOOH is inhibited only slightly by phenylalanine and not at all by 5-deaza-6-methyltetrahydropterin, a competitive inhibitor of phenylalanine hydroxylation. Phenylalanine 9-22 phenylalanine hydroxylase Rattus norvegicus 113-138 3356704-10 1988 LOOH and phenylalanine appear to react at different sites on phenylalanine appear to react at different sites on phenylalanine hydroxylase, and the reaction of LOOH is inhibited only slightly by phenylalanine and not at all by 5-deaza-6-methyltetrahydropterin, a competitive inhibitor of phenylalanine hydroxylation. Phenylalanine 61-74 phenylalanine hydroxylase Rattus norvegicus 113-138 3356704-10 1988 LOOH and phenylalanine appear to react at different sites on phenylalanine appear to react at different sites on phenylalanine hydroxylase, and the reaction of LOOH is inhibited only slightly by phenylalanine and not at all by 5-deaza-6-methyltetrahydropterin, a competitive inhibitor of phenylalanine hydroxylation. Phenylalanine 61-74 phenylalanine hydroxylase Rattus norvegicus 113-138 3356704-10 1988 LOOH and phenylalanine appear to react at different sites on phenylalanine appear to react at different sites on phenylalanine hydroxylase, and the reaction of LOOH is inhibited only slightly by phenylalanine and not at all by 5-deaza-6-methyltetrahydropterin, a competitive inhibitor of phenylalanine hydroxylation. Phenylalanine 61-74 phenylalanine hydroxylase Rattus norvegicus 113-138 2872885-7 1986 Phenylalanine hydroxylase was found to have a Control Coefficient for the degradation of phenylalanine of approx. Phenylalanine 89-102 phenylalanine hydroxylase Rattus norvegicus 0-25 3129035-6 1988 The Km value of phenylalanine for the cytoplasmic form of phenylalanine hydroxylase is 0.32.10(-3) M, that for the membrane form is 1.66.10(-3) M. Both enzyme forms can bind to phenyl-Sepharose after their activation by the substrate, and they dissociate from the carrier after phenylalanine removal from the incubation mixture, which points to the intactness of the phenylalanine binding allosteric center in the membrane form of the enzyme. Phenylalanine 16-29 phenylalanine hydroxylase Rattus norvegicus 58-83 3335542-7 1988 Phenylalanine hydroxylase at alkaline pH appears to be in an altered conformation that is very similar to that of the enzyme which has been activated by preincubation with phenylalanine as determined by changes in the intrinsic protein fluorescence spectrum of the enzyme. Phenylalanine 172-185 phenylalanine hydroxylase Rattus norvegicus 0-25 3335542-8 1988 Furthermore, phenylalanine hydroxylase which has been preincubated at an alkaline pH in the absence of phenylalanine and subsequently assayed at pH 7.0 in the presence of phenylalanine shows an increase in tetrahydrobiopterin-dependent activity similar to that exhibited by the enzyme which has been activated by preincubation with phenylalanine at neutral pH. Phenylalanine 103-116 phenylalanine hydroxylase Rattus norvegicus 13-38 3335542-8 1988 Furthermore, phenylalanine hydroxylase which has been preincubated at an alkaline pH in the absence of phenylalanine and subsequently assayed at pH 7.0 in the presence of phenylalanine shows an increase in tetrahydrobiopterin-dependent activity similar to that exhibited by the enzyme which has been activated by preincubation with phenylalanine at neutral pH. Phenylalanine 103-116 phenylalanine hydroxylase Rattus norvegicus 13-38 3722178-1 1986 Phenylalanine hydroxylase, the enzyme that catalyzes the irreversible hydroxylation of phenylalanine to tyrosine, was purified from rat kidney with the use of phenyl-Sepharose, DEAE-Sephacel, and gel permeation high pressure liquid chromatography. Phenylalanine 87-100 phenylalanine hydroxylase Rattus norvegicus 0-25 6681776-2 1983 High concentrations of phenylalanine were induced in pregnant rats from embryonic days 14 through 21 by subcutaneous injections of alpha-methylphenylalanine (mPhe) (to inhibit maternal phenylalanine hydroxylase) at a dosage of 30 mg/100 g body weight plus phenylalanine (Phe) supplementation (to raise fetal plasma phenylalanine) at a dosage of 60 mg/100 g body weight two times daily at 12-h intervals. Phenylalanine 23-36 phenylalanine hydroxylase Rattus norvegicus 185-210 4016080-1 1985 The formation of tyrosine from phenylalanine catalyzed by rat liver phenylalanine hydroxylase is coupled to the generation of a 4a-hydroxy adduct from the requisite tetrahydropterin cofactor. Phenylalanine 31-44 phenylalanine hydroxylase Rattus norvegicus 68-93 6186515-3 1983 In the first treatment, pregnant rats were injected subcutaneously with alpha-methylphenylalanine (to inhibit maternal liver phenylalanine hydroxylase) at a dosage of 30 mg/100 g body weight plus phenylalanine supplementation (to increase maternal and fetal plasma phenylalanine) at a dosage of 60 mg/100 g body weight two times daily. Phenylalanine 84-97 phenylalanine hydroxylase Rattus norvegicus 125-150 6186515-5 1983 Treatment with alpha-methylphenylalanine/phenylalanine (mPhe/Phe) resulted in a 76% inhibition in the activity of maternal phenylalanine hydroxylase and a 25-fold increase in the mean daily concentration of phenylalanine in the maternal and fetal plasma. Phenylalanine 27-40 phenylalanine hydroxylase Rattus norvegicus 123-148 6186515-5 1983 Treatment with alpha-methylphenylalanine/phenylalanine (mPhe/Phe) resulted in a 76% inhibition in the activity of maternal phenylalanine hydroxylase and a 25-fold increase in the mean daily concentration of phenylalanine in the maternal and fetal plasma. Phenylalanine 57-60 phenylalanine hydroxylase Rattus norvegicus 123-148 6186515-5 1983 Treatment with alpha-methylphenylalanine/phenylalanine (mPhe/Phe) resulted in a 76% inhibition in the activity of maternal phenylalanine hydroxylase and a 25-fold increase in the mean daily concentration of phenylalanine in the maternal and fetal plasma. Phenylalanine 41-54 phenylalanine hydroxylase Rattus norvegicus 123-148 4265522-3 1972 In young rats (13-15 days old), treatment with cortisol increased the activity of phenylalanine hydroxylase in the liver (measured in vitro) and accelerated the metabolism of administered phenylalanine: the rate constant of the disappearance of phenylalanine from plasma and the initial increase in tyrosine in plasma correlated quantitatively with the activity of phenylalanine hydroxylase in the liver. Phenylalanine 188-201 phenylalanine hydroxylase Rattus norvegicus 365-390 6838560-1 1983 The effects of phenylalanine and tetrahydrobiopterin on the limited proteolysis of rat liver phenylalanine hydroxylase by chymotrypsin have been examined. Phenylalanine 15-28 phenylalanine hydroxylase Rattus norvegicus 93-118 6838560-5 1983 Both tetrahydrobiopterin and phenylalanine inhibit the release of soluble radioactivity from [32P]phosphorylated phenylalanine hydroxylase. Phenylalanine 29-42 phenylalanine hydroxylase Rattus norvegicus 113-138 7240248-5 1981 For example, a change from sigmoid to hyperbolic kinetics with varying phenylalanine concentration is observed, in addition to broadened substrate specificity and a dependence on phenylalanine hydroxylase stimulator protein at pH 6.8. Phenylalanine 71-84 phenylalanine hydroxylase Rattus norvegicus 179-204 7240248-6 1981 The binding of phenylalanine to phenylalanine hydroxylase in the absence of pterin cofactor has also been studied. Phenylalanine 15-28 phenylalanine hydroxylase Rattus norvegicus 32-57 6257849-5 1981 Cerebral hyperglycinemia was also produced by chronic treatment with phenylalanine plus p-chlorophenylalanine to inhibit PAH, but not by acute (12 h) hyperphenylalaninemia. Phenylalanine 69-82 phenylalanine hydroxylase Rattus norvegicus 121-124 6257849-6 1981 An increase in cerebral phosphoserine phosphatase activity was greater in rats treated with phenylalanine plus PAH inhibitor than with inhibitor alone. Phenylalanine 92-105 phenylalanine hydroxylase Rattus norvegicus 111-114 6446685-5 1980 Most successful is the simultaneous application to developing rats of alpha-methyl-phenylalanine (an inhibitor of phenylalanine hydroxylase), together with phenylalanine. Phenylalanine 83-96 phenylalanine hydroxylase Rattus norvegicus 114-139 728481-0 1978 Phenylalanine analogues as inhibitors of phenylalanine-hydroxylase from rat liver. Phenylalanine 0-13 phenylalanine hydroxylase Rattus norvegicus 41-66 728481-2 1978 The conversion of phenylalanine to tyrosine is catalysed by phenylalanine-hydroxylase. Phenylalanine 18-31 phenylalanine hydroxylase Rattus norvegicus 60-85 145879-3 1977 Combination of p.chlorophenylalanine, strongly inhibitor of phenylalanine hydroxylase, and cotrimoxazole, presumably inhibitor of dihydropteridine reductase, produced a good inhibition of phenylalanine hydroxylation in vivo. Phenylalanine 23-36 phenylalanine hydroxylase Rattus norvegicus 60-85 133671-2 1976 Injections of phenylalanine increased a 2.5-fold in 9 h the hepatic phenylalanine hydroxylase activity of 6-day-old or adult rats that had been pretreated (24h earlier) with p-chlorophenylalanine; without such pretreatment, phenylalanine did not raise the enzyme concentration. Phenylalanine 14-27 phenylalanine hydroxylase Rattus norvegicus 68-93 124733-7 1975 Randomly ring-tritiated phenylalanine can be used interchangeably with ring-deuterated phenylalanine if greater sensitivity is needed in the in vivo assay for phenylalanine hydroxylase. Phenylalanine 24-37 phenylalanine hydroxylase Rattus norvegicus 159-184 4260277-2 1972 This model uses inhibition in rats of phenylalanine hydroxylase (EC 1.14.3.1) by p-chlorophenylalanine and supplementation with phenylalanine to produce a high ratio of phenylalanine to tyrosine in their blood. Phenylalanine 89-102 phenylalanine hydroxylase Rattus norvegicus 38-63 6981644-1 1982 We show that phenylalanine is able to control the extent of activation and, as a result, the catalytic activity of rat liver phenylalanine hydroxylase in vivo, in perfused liver, and in vitro. Phenylalanine 13-26 phenylalanine hydroxylase Rattus norvegicus 125-150 7430114-2 1980 In the experiments presented, the stoichiometry of binding of phenylalanine to activated rat liver phenylalanine hydroxylase was measured. Phenylalanine 62-75 phenylalanine hydroxylase Rattus norvegicus 99-124 23386-3 1978 Conversion of phenylalanine to tyrosine was measured in living cells by chromatographic identification of the metabolites of [14C]phenylalanine and in cell extracts using a sensitive assay for phenylalanine hydroxylase. Phenylalanine 14-27 phenylalanine hydroxylase Rattus norvegicus 193-218 4854919-8 1974 The K(m) values for phenylalanine and cofactor were respectively one-quarter and twice those found for rat liver phenylalanine hydroxylase. Phenylalanine 20-33 phenylalanine hydroxylase Rattus norvegicus 113-138 20307070-1 2010 Phenylalanine acts as an allosteric activator of the tetrahydropterin-dependent enzyme phenylalanine hydroxylase. Phenylalanine 0-13 phenylalanine hydroxylase Rattus norvegicus 87-112 6067632-0 1967 The effect of phenylalanine administration on the activities of phenylalanine hydroxylase, some aminotransferases and decarboxylases in adult rats. Phenylalanine 14-27 phenylalanine hydroxylase Rattus norvegicus 64-89 14193366-0 1964 EFFECT OF DIETARY PHENYLALANINE ON ACTIVITY OF PHENYLALANINE HYDROXYLASE FROM RAT LIVER. Phenylalanine 18-31 phenylalanine hydroxylase Rattus norvegicus 47-72 26823465-0 2016 Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase. Phenylalanine 42-55 phenylalanine hydroxylase Rattus norvegicus 63-88 26823465-1 2016 Liver phenylalanine hydroxylase (PheH) is an allosteric enzyme that requires activation by phenylalanine for full activity. Phenylalanine 6-19 phenylalanine hydroxylase Rattus norvegicus 33-37 26823465-3 2016 NMR spectroscopy of the isolated regulatory domain (RDPheH(25-117) is the regulatory domain of PheH lacking residues 1-24) of the rat enzyme in the presence of phenylalanine is consistent with formation of a side-by-side ACT dimer. Phenylalanine 160-173 phenylalanine hydroxylase Rattus norvegicus 54-58 20951114-0 2011 Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase. Phenylalanine 22-35 phenylalanine hydroxylase Rattus norvegicus 69-94 20951114-1 2011 The hydroxylation of phenylalanine to tyrosine by the liver enzyme phenylalanine hydroxylase is regulated by the level of phenylalanine. Phenylalanine 21-34 phenylalanine hydroxylase Rattus norvegicus 67-92 16953590-1 2006 Phenylalanine hydroxylase (PheH) and tryptophan hydroxylase (TrpH) catalyze the aromatic hydroxylation of phenylalanine and tryptophan, forming tyrosine and 5-hydroxytryptophan, respectively. Phenylalanine 106-119 phenylalanine hydroxylase Rattus norvegicus 0-25 16953590-1 2006 Phenylalanine hydroxylase (PheH) and tryptophan hydroxylase (TrpH) catalyze the aromatic hydroxylation of phenylalanine and tryptophan, forming tyrosine and 5-hydroxytryptophan, respectively. Phenylalanine 106-119 phenylalanine hydroxylase Rattus norvegicus 27-31