PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12379147-7 2003 The binding isotherm for tetrameric and dimeric wt-hPAH revealed a [S](0.5)-value of 98+/-7 microM (h =1.0) and 158+/-11 microM, respectively, i.e. for the tetramer it is slightly lower than the value (145+/-5 microM) obtained for the co-operative binding (h =1.6+/-0.4) of L-Phe as measured by the change in intrinsic tryptophan fluorescence. Tryptophan 319-329 phenylalanine hydroxylase Homo sapiens 51-55 11747434-6 2001 The resulting ternary TPH-BH2-L-Trp structure is very similar to that previously determined by the same methods for the complex of phenylalanine hydroxylase (PAH) with BH2 and L-Phe [Teigen, K., et al. Tryptophan 30-35 phenylalanine hydroxylase Homo sapiens 131-156 11747434-6 2001 The resulting ternary TPH-BH2-L-Trp structure is very similar to that previously determined by the same methods for the complex of phenylalanine hydroxylase (PAH) with BH2 and L-Phe [Teigen, K., et al. Tryptophan 30-35 phenylalanine hydroxylase Homo sapiens 158-161 11747434-13 2001 Moreover, Phe313, which seems to interact with the substrate through ring stacking, corresponds to a Trp residue in both tyrosine hydroxylase and PAH (Trp326) and appears to be an important residue for influencing the substrate specificity in this family of enzymes. Tryptophan 101-104 phenylalanine hydroxylase Homo sapiens 146-149 11747434-14 2001 We show that the W326F mutation in PAH increases the relative preference for L-Trp as the substrate, while the F313W mutation in TPH increases the preference for L-Phe, possibly by a conserved active site volume effect. Tryptophan 77-82 phenylalanine hydroxylase Homo sapiens 35-38 9022714-9 1996 The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH. Tryptophan 176-186 phenylalanine hydroxylase Homo sapiens 36-40 9022714-9 1996 The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH. Tryptophan 176-186 phenylalanine hydroxylase Homo sapiens 60-64 9022714-9 1996 The amino-terminal deletion mutants hPAH(Asp112-Lys452) and hPAH(Gly103-Gln428) revealed high specific activity, increased apparent affinity for L-Phe (S0.5 = 60 microM) and a tryptophan fluorescence emission spectrum similar to that of the L-Phe-activated wt-hPAH. Tryptophan 176-186 phenylalanine hydroxylase Homo sapiens 60-64 7547912-0 1995 Tryptophan fluorescence of human phenylalanine hydroxylase produced in Escherichia coli. Tryptophan 0-10 phenylalanine hydroxylase Homo sapiens 33-58 7547912-1 1995 Human phenylalanine hydroxylase (hPAH) contains three tryptophan residues (W120, W187, and W326). Tryptophan 54-64 phenylalanine hydroxylase Homo sapiens 6-31 7547912-1 1995 Human phenylalanine hydroxylase (hPAH) contains three tryptophan residues (W120, W187, and W326). Tryptophan 54-64 phenylalanine hydroxylase Homo sapiens 33-37 7547912-7 1995 On the basis of measurements of mutants containing only one tryptophan, it was calculated that W120, W187, and W326 account for approximately 61, 13, and 26% of the total tryptophan fluorescence of hPAH, respectively, while the positions of the emission maxima (335.5-336.5 nm) and the widths at half-height (55-60 nm) of the emission spectra of the individual tryptophans were rather similar. Tryptophan 60-70 phenylalanine hydroxylase Homo sapiens 198-202 7547912-7 1995 On the basis of measurements of mutants containing only one tryptophan, it was calculated that W120, W187, and W326 account for approximately 61, 13, and 26% of the total tryptophan fluorescence of hPAH, respectively, while the positions of the emission maxima (335.5-336.5 nm) and the widths at half-height (55-60 nm) of the emission spectra of the individual tryptophans were rather similar. Tryptophan 171-181 phenylalanine hydroxylase Homo sapiens 198-202 7547912-7 1995 On the basis of measurements of mutants containing only one tryptophan, it was calculated that W120, W187, and W326 account for approximately 61, 13, and 26% of the total tryptophan fluorescence of hPAH, respectively, while the positions of the emission maxima (335.5-336.5 nm) and the widths at half-height (55-60 nm) of the emission spectra of the individual tryptophans were rather similar. Tryptophan 361-372 phenylalanine hydroxylase Homo sapiens 198-202 6487579-9 1984 These results suggest that activation of phenylalanine hydroxylase results in a conformation change and the exposure of buried tryptophan(s) and possibly a cysteine residue. Tryptophan 127-137 phenylalanine hydroxylase Homo sapiens 41-66 5686299-0 1968 Phenylalanine hydroxylase activity towards two substrates simultaneously: enhancement of inhibition by phenylalanine, tryptophan and their derivatives. Tryptophan 118-128 phenylalanine hydroxylase Homo sapiens 0-25 22112818-9 2012 The p.R408W mutation, in which substitution of straight chain arginine with bulky aromatic amine, tryptophan, at the crux of a strategic hinge site activating folding of PAH, amino acid sequence 408, was strongly associated with non-response (21/29 patients non-responsive, 12/17 genotypes non-responsive). Tryptophan 98-108 phenylalanine hydroxylase Homo sapiens 170-173 2889273-4 1987 The locations of these genes and the evolutionary distance between their sequences suggest that at least three distinct genetic events have occurred during the evolution of the aromatic amino acid hydroxylase superfamily: two sequential gene duplications giving rise to the three distinct hydroxylase loci, and a translocation which separated the tryptophan and tyrosine hydroxylase loci on chromosome 11 from the phenylalanine hydroxylase locus on chromosome 12. Tryptophan 347-357 phenylalanine hydroxylase Homo sapiens 414-439 14491501-0 1962 Hydroxylation of tryptophan by phenylalanine hydroxylase. Tryptophan 17-27 phenylalanine hydroxylase Homo sapiens 31-56 15060071-3 2004 On this basis, single-site mutagenesis of key residues in these regions of the human PAH tetramer was performed in the present study, and their functional impact was measured by steady-state kinetics and the global conformational transition as assessed by surface plasmon resonance and intrinsic tryptophan fluorescence spectroscopy. Tryptophan 296-306 phenylalanine hydroxylase Homo sapiens 85-88