Articles - 1j8t mentioned but not cited (2)
- Loss of function in phenylketonuria is caused by impaired molecular motions and conformational instability. Gersting SW, Kemter KF, Staudigl M, Messing DD, Danecka MK, Lagler FB, Sommerhoff CP, Roscher AA, Muntau AC. Am J Hum Genet 83 5-17 (2008)
- Unravelling the Complex Denaturant and Thermal-Induced Unfolding Equilibria of Human Phenylalanine Hydroxylase. Conde-Giménez M, Sancho J. Int J Mol Sci 22 6539 (2021)
Reviews citing this publication (8)
- Mononuclear non-heme iron enzymes with the 2-His-1-carboxylate facial triad: recent developments in enzymology and modeling studies. Bruijnincx PC, van Koten G, Klein Gebbink RJ. Chem Soc Rev 37 2716-2744 (2008)
- Mechanism of aromatic amino acid hydroxylation. Fitzpatrick PF. Biochemistry 42 14083-14091 (2003)
- Non-heme iron oxygenases. Ryle MJ, Hausinger RP. Curr Opin Chem Biol 6 193-201 (2002)
- PAHdb 2003: what a locus-specific knowledgebase can do. Scriver CR, Hurtubise M, Konecki D, Phommarinh M, Prevost L, Erlandsen H, Stevens R, Waters PJ, Ryan S, McDonald D, Sarkissian C. Hum Mutat 21 333-344 (2003)
- How PAH gene mutations cause hyper-phenylalaninemia and why mechanism matters: insights from in vitro expression. Waters PJ. Hum Mutat 21 357-369 (2003)
- Allosteric regulation of phenylalanine hydroxylase. Fitzpatrick PF. Arch Biochem Biophys 519 194-201 (2012)
- Phenylketonuria as a model for protein misfolding diseases and for the development of next generation orphan drugs for patients with inborn errors of metabolism. Muntau AC, Gersting SW. J Inherit Metab Dis 33 649-658 (2010)
- New protein structures provide an updated understanding of phenylketonuria. Jaffe EK. Mol Genet Metab 121 289-296 (2017)
Articles citing this publication (47)
- Correction of kinetic and stability defects by tetrahydrobiopterin in phenylketonuria patients with certain phenylalanine hydroxylase mutations. Erlandsen H, Pey AL, Gámez A, Pérez B, Desviat LR, Aguado C, Koch R, Surendran S, Tyring S, Matalon R, Scriver CR, Ugarte M, Martínez A, Stevens RC. Proc Natl Acad Sci U S A 101 16903-16908 (2004)
- Predicted effects of missense mutations on native-state stability account for phenotypic outcome in phenylketonuria, a paradigm of misfolding diseases. Pey AL, Stricher F, Serrano L, Martinez A. Am J Hum Genet 81 1006-1024 (2007)
- Crystal structure of the ternary complex of the catalytic domain of human phenylalanine hydroxylase with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine, and its implications for the mechanism of catalysis and substrate activation. Andersen OA, Flatmark T, Hough E. J Mol Biol 320 1095-1108 (2002)
- VTVH-MCD and DFT studies of thiolate bonding to [FeNO]7/[FeO2]8 complexes of isopenicillin N synthase: substrate determination of oxidase versus oxygenase activity in nonheme Fe enzymes. Brown CD, Neidig ML, Neibergall MB, Lipscomb JD, Solomon EI. J Am Chem Soc 129 7427-7438 (2007)
- 2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding. Andersen OA, Stokka AJ, Flatmark T, Hough E. J Mol Biol 333 747-757 (2003)
- Evidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylase. Panay AJ, Lee M, Krebs C, Bollinger JM, Fitzpatrick PF. Biochemistry 50 1928-1933 (2011)
- Structural comparison of bacterial and human iron-dependent phenylalanine hydroxylases: similar fold, different stability and reaction rates. Erlandsen H, Kim JY, Patch MG, Han A, Volner A, Abu-Omar MM, Stevens RC. J Mol Biol 320 645-661 (2002)
- Structural perturbations in the Ala --> Val polymorphism of methylenetetrahydrofolate reductase: how binding of folates may protect against inactivation. Pejchal R, Campbell E, Guenther BD, Lennon BW, Matthews RG, Ludwig ML. Biochemistry 45 4808-4818 (2006)
- Linking genotypes database with locus-specific database and genotype-phenotype correlation in phenylketonuria. Wettstein S, Underhaug J, Perez B, Marsden BD, Yue WW, Martinez A, Blau N. Eur J Hum Genet 23 302-309 (2015)
- Pahenu1 is a mouse model for tetrahydrobiopterin-responsive phenylalanine hydroxylase deficiency and promotes analysis of the pharmacological chaperone mechanism in vivo. Gersting SW, Lagler FB, Eichinger A, Kemter KF, Danecka MK, Messing DD, Staudigl M, Domdey KA, Zsifkovits C, Fingerhut R, Glossmann H, Roscher AA, Muntau AC. Hum Mol Genet 19 2039-2049 (2010)
- Reduction and oxidation of the active site iron in tyrosine hydroxylase: kinetics and specificity. Frantom PA, Seravalli J, Ragsdale SW, Fitzpatrick PF. Biochemistry 45 2372-2379 (2006)
- Spectroscopic studies of the mononuclear non-heme Fe(II) enzyme FIH: second-sphere contributions to reactivity. Light KM, Hangasky JA, Knapp MJ, Solomon EI. J Am Chem Soc 135 9665-9674 (2013)
- Identification of phenylalanine 3-hydroxylase for meta-tyrosine biosynthesis. Zhang W, Ames BD, Walsh CT. Biochemistry 50 5401-5403 (2011)
- Accurate prediction of functional effects for variants by combining gradient tree boosting with optimal neighborhood properties. Pan Y, Liu D, Deng L. PLoS One 12 e0179314 (2017)
- Structure of full-length human phenylalanine hydroxylase in complex with tetrahydrobiopterin. Flydal MI, Alcorlo-Pagés M, Johannessen FG, Martínez-Caballero S, Skjærven L, Fernandez-Leiro R, Martinez A, Hermoso JA. Proc Natl Acad Sci U S A 116 11229-11234 (2019)
- Studies on the regulatory properties of the pterin cofactor and dopamine bound at the active site of human phenylalanine hydroxylase. Solstad T, Stokka AJ, Andersen OA, Flatmark T. Eur J Biochem 270 981-990 (2003)
- A Mononuclear Carboxylate-Rich Oxoiron(IV) Complex: a Structural and Functional Mimic of TauD Intermediate 'J' McDonald AR, Guo Y, Vu VV, Bominaar EL, Münck E, Que L. Chem Sci 3 1680-1693 (2012)
- Role of the phenylalanine-hydroxylating system in aromatic substance degradation and lipid metabolism in the oleaginous fungus Mortierella alpina. Wang H, Chen H, Hao G, Yang B, Feng Y, Wang Y, Feng L, Zhao J, Song Y, Zhang H, Chen YQ, Wang L, Chen W. Appl Environ Microbiol 79 3225-3233 (2013)
- Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps. Frantom PA, Fitzpatrick PF. J Am Chem Soc 125 16190-16191 (2003)
- Dynamic regulation of phenylalanine hydroxylase by simulated redox manipulation. Fuchs JE, Huber RG, von Grafenstein S, Wallnoefer HG, Spitzer GM, Fuchs D, Liedl KR. PLoS One 7 e53005 (2012)
- Probing the role of crystallographically defined/predicted hinge-bending regions in the substrate-induced global conformational transition and catalytic activation of human phenylalanine hydroxylase by single-site mutagenesis. Stokka AJ, Carvalho RN, Barroso JF, Flatmark T. J Biol Chem 279 26571-26580 (2004)
- Substrate-induced conformational transition in human phenylalanine hydroxylase as studied by surface plasmon resonance analyses: the effect of terminal deletions, substrate analogues and phosphorylation. Stokka AJ, Flatmark T. Biochem J 369 509-518 (2003)
- Effects of ligands on the mobility of an active-site loop in tyrosine hydroxylase as monitored by fluorescence anisotropy. Sura GR, Lasagna M, Gawandi V, Reinhart GD, Fitzpatrick PF. Biochemistry 45 9632-9638 (2006)
- Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments. Roberts KM, Pavon JA, Fitzpatrick PF. Biochemistry 52 1062-1073 (2013)
- Mechanism of Inhibition of Novel Tryptophan Hydroxylase Inhibitors Revealed by Co-crystal Structures and Kinetic Analysis. Cianchetta G, Stouch T, Yu W, Shi ZC, Tari LW, Swanson RV, Hunter MJ, Hoffman ID, Liu Q. Curr Chem Genomics 4 19-26 (2010)
- A flexible loop in tyrosine hydroxylase controls coupling of amino acid hydroxylation to tetrahydropterin oxidation. Daubner SC, McGinnis JT, Gardner M, Kroboth SL, Morris AR, Fitzpatrick PF. J Mol Biol 359 299-307 (2006)
- Probing cofactor specificity in phenylalanine hydroxylase by molecular dynamics simulations. Teigen K, Martinez A. J Biomol Struct Dyn 20 733-740 (2003)
- Biophysical characterization of full-length human phenylalanine hydroxylase provides a deeper understanding of its quaternary structure equilibrium. Arturo EC, Gupta K, Hansen MR, Borne E, Jaffe EK. J Biol Chem 294 10131-10145 (2019)
- Pulsed EPR study of amino acid and tetrahydropterin binding in a tyrosine hydroxylase nitric oxide complex: evidence for substrate rearrangements in the formation of the oxygen-reactive complex. Krzyaniak MD, Eser BE, Ellis HR, Fitzpatrick PF, McCracken J. Biochemistry 52 8430-8441 (2013)
- Artificial Iron Proteins: Modeling the Active Sites in Non-Heme Dioxygenases. Miller KR, Paretsky JD, Follmer AH, Heinisch T, Mittra K, Gul S, Kim IS, Fuller FD, Batyuk A, Sutherlin KD, Brewster AS, Bhowmick A, Sauter NK, Kern J, Yano J, Green MT, Ward TR, Borovik AS. Inorg Chem 59 6000-6009 (2020)
- The structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes. Acharya P, Warkentin E, Ermler U, Thauer RK, Shima S. J Mol Biol 357 870-879 (2006)
- Formation of the iron-oxo hydroxylating species in the catalytic cycle of aromatic amino acid hydroxylases. Olsson E, Martinez A, Teigen K, Jensen VR. Chemistry 17 3746-3758 (2011)
- Characterization of metal ligand mutants of phenylalanine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad. Li J, Fitzpatrick PF. Arch Biochem Biophys 475 164-168 (2008)
- Structure of full-length wild-type human phenylalanine hydroxylase by small angle X-ray scattering reveals substrate-induced conformational stability. Tomé CS, Lopes RR, Sousa PMF, Amaro MP, Leandro J, Mertens HDT, Leandro P, Vicente JB. Sci Rep 9 13615 (2019)
- Proton shift upon one-electron reduction in ruthenium(II)-coordinated pterins. Miyazaki S, Ohkubo K, Kojima T, Fukuzumi S. Angew Chem Int Ed Engl 47 9669-9672 (2008)
- Direct coordination of pterin to FeII enables neurotransmitter biosynthesis in the pterin-dependent hydroxylases. Iyer SR, Tidemand KD, Babicz JT, Jacobs AB, Gee LB, Haahr LT, Yoda Y, Kurokuzu M, Kitao S, Saito M, Seto M, Christensen HEM, Peters GHJ, Solomon EI. Proc Natl Acad Sci U S A 118 e2022379118 (2021)
- Stabilization of tryptophan hydroxylase 2 by l-phenylalanine-induced dimerization. Tidemand KD, Christensen HE, Hoeck N, Harris P, Boesen J, Peters GH. FEBS Open Bio 6 987-999 (2016)
- A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis. Ronau JA, Paul LN, Fuchs JE, Liedl KR, Abu-Omar MM, Das C. Biochemistry 53 6834-6848 (2014)
- Substituting Tyr138 in the active site loop of human phenylalanine hydroxylase affects catalysis and substrate activation. Leandro J, Stokka AJ, Teigen K, Andersen OA, Flatmark T. FEBS Open Bio 7 1026-1036 (2017)
- The regulatory domain of human tryptophan hydroxylase 1 forms a stable dimer. Zhang S, Hinck CS, Fitzpatrick PF. Biochem Biophys Res Commun 476 457-461 (2016)
- XANES study of the carboxylate binding mode in two pterin hydroxylases. Mijovilovich A. Chem Biodivers 5 2131-2139 (2008)
- A simple method to calculate the accessible volume of protein-bound ligands: application for ligand selectivity. Hodneland E, Teigen K. J Mol Graph Model 26 429-433 (2007)
- In silico analyses of the effects of a point mutation and a pharmacological chaperone on the thermal fluctuation of phenylalanine hydroxylase. Hayakawa D, Hayakawa D, Yamaotsu N, Nakagome I, Ozawa SI, Yoshida T, Hirono S. Biophys Chem 228 47-54 (2017)
- Spectroscopic characterization of Cu(II) complex of L-phenylalanine and D,L-tryptophan. Altun O, Bilcen S. Spectrochim Acta A Mol Biomol Spectrosc 75 789-793 (2010)
- Structural and thermodynamic insight into phenylalanine hydroxylase from the human pathogen Legionella pneumophila. Leiros HK, Flydal MI, Martinez A. FEBS Open Bio 3 370-378 (2013)
- Letter The possible substrate inhibition of epidermal phenylalanine hydroxylase in vitiligo: a new pathogenetic approach. Batcioglu K, Hazneci E. Med Hypotheses 63 918-919 (2004)
- Thermodynamics of iron, tetrahydrobiopterin, and phenylalanine binding to phenylalanine hydroxylase from Chromobacterium violaceum. Li M, Subedi BP, Fitzpatrick PF, Emerson JP. Arch Biochem Biophys 729 109378 (2022)