| Year |
Citation |
Score |
| 2023 |
Fitzpatrick PF. The aromatic amino acid hydroxylases: Structures, catalysis, and regulation of phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase. Archives of Biochemistry and Biophysics. 735: 109518. PMID 36639008 DOI: 10.1016/j.abb.2023.109518 |
0.345 |
|
| 2022 |
Li M, Subedi BP, Fitzpatrick PF, Emerson JP. Thermodynamics of iron, tetrahydrobiopterin, and phenylalanine binding to phenylalanine hydroxylase from Chromobacterium violaceum. Archives of Biochemistry and Biophysics. 109378. PMID 35995215 DOI: 10.1016/j.abb.2022.109378 |
0.326 |
|
| 2019 |
Wanninayake US, Subedi B, Fitzpatrick PF. pH and deuterium isotope effects on the reaction of trimethylamine dehydrogenase with dimethylamine. Archives of Biochemistry and Biophysics. 108136. PMID 31604072 DOI: 10.1016/J.Abb.2019.108136 |
0.433 |
|
| 2019 |
Fitzpatrick PF, Dougherty V, Subedi B, Quilantan J, Hinck CS, Lujan AI, Tormos JR. The mechanism of the flavoprotein D-6-hydroxynicotine oxidase: substrate specificity, pH and solvent isotope effects, and roles of key active-site residues. Biochemistry. PMID 31046245 DOI: 10.1021/Acs.Biochem.9B00297 |
0.471 |
|
| 2019 |
Khan CA, Meisburger SP, Ando N, Fitzpatrick PF. The phenylketonuria-associated substitution R68S converts phenylalanine hydroxylase to a constitutively active enzyme but reduces its stability. The Journal of Biological Chemistry. PMID 30674554 DOI: 10.1074/Jbc.Ra118.006477 |
0.809 |
|
| 2018 |
Khan CA, Fitzpatrick PF. Phosphorylation of phenylalanine hydroxylase increases the rate constant for formation of the activated conformation of the enzyme. Biochemistry. PMID 30346142 DOI: 10.1021/Acs.Biochem.8B00919 |
0.82 |
|
| 2018 |
Fitzpatrick PF. The enzymes of microbial nicotine metabolism. Beilstein Journal of Organic Chemistry. 14: 2295-2307. PMID 30202483 DOI: 10.3762/Bjoc.14.204 |
0.319 |
|
| 2018 |
Halling P, Fitzpatrick PF, Raushel FM, Rohwer J, Schnell S, Wittig U, Wohlgemuth R, Kettner C. An empirical analysis of enzyme function reporting for experimental reproducibility: Missing/incomplete information in published papers. Biophysical Chemistry. 242: 22-27. PMID 30195215 DOI: 10.1016/J.Bpc.2018.08.004 |
0.564 |
|
| 2018 |
Subedi BP, Fitzpatrick PF. Mutagenesis of an active-site loop in tryptophan hydroxylase dra-matically slows the formation of an early intermediate in catalysis. Journal of the American Chemical Society. PMID 29589922 DOI: 10.1021/Jacs.8B00936 |
0.508 |
|
| 2018 |
Swainston N, Baici A, Bakker BM, Cornish-Bowden A, Fitzpatrick PF, Halling P, Leyh TS, O'Donovan C, Raushel FM, Reschel U, Rohwer JM, Schnell S, Schomburg D, Tipton KF, Tsai MD, et al. STRENDA DB: enabling the validation and sharing of enzyme kinetics data. The Febs Journal. PMID 29498804 DOI: 10.1111/Febs.14427 |
0.519 |
|
| 2017 |
Roberts KM, Fitzpatrick PF. Measurement of Kinetic Isotope Effects in an Enzyme-Catalyzed Reaction by Continuous-Flow Mass Spectrometry. Methods in Enzymology. 596: 149-161. PMID 28911769 DOI: 10.1016/Bs.Mie.2017.07.001 |
0.726 |
|
| 2017 |
Taylor AB, Roberts KM, Cao X, Clark NE, Holloway SP, Donati E, Polcaro CM, Pica-Mattoccia L, Tarpley RS, McHardy SF, Cioli D, LoVerde PT, Fitzpatrick PF, Hart PJ. Structural and Enzymatic Insights into Species-specific Resistance to Schistosome Parasite Drug Therapy. The Journal of Biological Chemistry. PMID 28536265 DOI: 10.1074/Jbc.M116.766527 |
0.671 |
|
| 2017 |
Fitzpatrick PF. Nitroalkane oxidase: Structure and mechanism. Archives of Biochemistry and Biophysics. PMID 28529198 DOI: 10.1016/J.Abb.2017.05.012 |
0.368 |
|
| 2017 |
Trimmer EE, Wanninayake U, Fitzpatrick PF. Mechanistic Studies of an Amine Oxidase Derived from D-Amino Acid Oxidase. Biochemistry. PMID 28355481 DOI: 10.1021/Acs.Biochem.7B00161 |
0.504 |
|
| 2017 |
Fitzpatrick PF, Chadegani F, Zhang S, Dougherty V. The mechanism of the flavoprotein 6-hydroxy-L-nicotine oxidase: pH and solvent isotope effects and identification of key active site residues. Biochemistry. PMID 28080034 DOI: 10.1021/Acs.Biochem.6B01160 |
0.463 |
|
| 2017 |
Meisburger S, Taylor A, Khan C, Zhang S, Fitzpatrick P, Ando N. A new method for computational purification of complex mixtures by chromatography-coupled SAXS Acta Crystallographica Section a Foundations and Advances. 73: a119-a119. DOI: 10.1107/S0108767317098816 |
0.748 |
|
| 2016 |
Subedi BP, Fitzpatrick PF. Kinetic Mechanism and Intrinsic Rate Constants for the Reaction of a Bacterial Phenylalanine Hydroxylase. Biochemistry. 55: 6848-6857. PMID 27951651 DOI: 10.1021/Acs.Biochem.6B01012 |
0.503 |
|
| 2016 |
Clark NE, Katolik A, Roberts KM, Taylor AB, Holloway SP, Schuermann JP, Montemayor EJ, Stevens SW, Fitzpatrick PF, Damha MJ, Hart PJ. Metal dependence and branched RNA cocrystal structures of the RNA lariat debranching enzyme Dbr1. Proceedings of the National Academy of Sciences of the United States of America. PMID 27930312 DOI: 10.1073/Pnas.1612729114 |
0.704 |
|
| 2016 |
Tormos JR, Suarez MB, Fitzpatrick PF. (13)C kinetic isotope effects on the reaction of a flavin amine oxidase determined from whole molecule isotope effects. Archives of Biochemistry and Biophysics. 612: 115-119. PMID 27815088 DOI: 10.1016/J.Abb.2016.10.018 |
0.416 |
|
| 2016 |
Becher I, Werner T, Doce C, Zaal EA, Tögel I, Khan CA, Rueger A, Muelbaier M, Salzer E, Berkers CR, Fitzpatrick PF, Bantscheff M, Savitski MM. Thermal profiling reveals phenylalanine hydroxylase as an off-target of panobinostat. Nature Chemical Biology. PMID 27669419 DOI: 10.1038/Nchembio.2185 |
0.761 |
|
| 2016 |
Zhang S, Hinck CS, Fitzpatrick PF. The regulatory domain of human tryptophan Hydroxylase 1 forms a stable dimer. Biochemical and Biophysical Research Communications. PMID 27255998 DOI: 10.1016/J.Bbrc.2016.05.144 |
0.414 |
|
| 2016 |
Meisburger SP, Taylor AB, Khan CA, Zhang S, Fitzpatrick PF, Ando N. Domain movements upon activation of phenylalanine hydroxylase characterized by crystallography and chromatography-coupled small-angle X-ray scattering. Journal of the American Chemical Society. PMID 27145334 DOI: 10.1021/Jacs.6B01563 |
0.804 |
|
| 2016 |
Zhang S, Fitzpatrick PF. Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase. The Journal of Biological Chemistry. PMID 26823465 DOI: 10.1074/Jbc.M115.709998 |
0.435 |
|
| 2016 |
Fitzpatrick PF, Chadegani F, Zhang S, Roberts KM, Hinck CS. The mechanism of the flavoprotein L-hydroxynicotine oxidase: kinetic mechanism, substrate specificity, reaction product, and roles of active site residues. Biochemistry. PMID 26744768 DOI: 10.1021/Acs.Biochem.5B01325 |
0.759 |
|
| 2015 |
Zhang S, Hinck AP, Fitzpatrick PF. The Amino Acid Specificity for Activation of Phenylalanine Hydroxylase Matches the Specificity for Stabilization of Regulatory Domain Dimers. Biochemistry. PMID 26252467 DOI: 10.1021/Acs.Biochem.5B00616 |
0.421 |
|
| 2015 |
Fitzpatrick PF. Structural insights into the regulation of aromatic amino acid hydroxylation. Current Opinion in Structural Biology. 35: 1-6. PMID 26241318 DOI: 10.1016/J.Sbi.2015.07.004 |
0.422 |
|
| 2015 |
McCracken J, Eser BE, Mannikko D, Krzyaniak MD, Fitzpatrick PF. HYSCORE Analysis of the Effects of Substrates on Coordination of Water to the Active Site Iron in Tyrosine Hydroxylase. Biochemistry. 54: 3759-71. PMID 26024204 DOI: 10.1021/Acs.Biochem.5B00363 |
0.379 |
|
| 2014 |
Roberts KM, Khan CA, Hinck CS, Fitzpatrick PF. Activation of phenylalanine hydroxylase by phenylalanine does not require binding in the active site. Biochemistry. 53: 7846-53. PMID 25453233 DOI: 10.1021/Bi501183X |
0.824 |
|
| 2014 |
Fitzpatrick PF. Combining solvent isotope effects with substrate isotope effects in mechanistic studies of alcohol and amine oxidation by enzymes. Biochimica Et Biophysica Acta. PMID 25448013 DOI: 10.1016/J.Bbapap.2014.10.020 |
0.421 |
|
| 2014 |
Zhang S, Roberts KM, Fitzpatrick PF. Phenylalanine binding is linked to dimerization of the regulatory domain of phenylalanine hydroxylase. Biochemistry. 53: 6625-7. PMID 25299136 DOI: 10.1021/Bi501109S |
0.738 |
|
| 2014 |
Roberts KM, Tormos JR, Fitzpatrick PF. Characterization of unstable products of flavin- and pterin-dependent enzymes by continuous-flow mass spectrometry. Biochemistry. 53: 2672-9. PMID 24713088 DOI: 10.1021/Bi500267C |
0.728 |
|
| 2014 |
Zhang S, Huang T, Ilangovan U, Hinck AP, Fitzpatrick PF. The solution structure of the regulatory domain of tyrosine hydroxylase. Journal of Molecular Biology. 426: 1483-97. PMID 24361276 DOI: 10.1016/J.Jmb.2013.12.015 |
0.354 |
|
| 2013 |
Krzyaniak MD, Eser BE, Ellis HR, Fitzpatrick PF, McCracken J. 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. Biochemistry. 52: 8430-41. PMID 24168553 DOI: 10.1021/Bi4010914 |
0.76 |
|
| 2013 |
Gadda G, Fitzpatrick PF. Solvent isotope and viscosity effects on the steady-state kinetics of the flavoprotein nitroalkane oxidase. Febs Letters. 587: 2785-9. PMID 23660407 DOI: 10.1016/J.Febslet.2013.04.021 |
0.593 |
|
| 2013 |
Li J, Fitzpatrick PF. Regulation of phenylalanine hydroxylase: conformational changes upon phosphorylation detected by H/D exchange and mass spectrometry. Archives of Biochemistry and Biophysics. 535: 115-9. PMID 23537590 DOI: 10.1016/J.Abb.2013.03.006 |
0.433 |
|
| 2013 |
Gaweska HM, Taylor AB, Hart PJ, Fitzpatrick PF. Structure of the flavoprotein tryptophan 2-monooxygenase, a key enzyme in the formation of galls in plants. Biochemistry. 52: 2620-6. PMID 23521653 DOI: 10.1021/Bi4001563 |
0.498 |
|
| 2013 |
Roberts KM, Fitzpatrick PF. Mechanisms of tryptophan and tyrosine hydroxylase. Iubmb Life. 65: 350-7. PMID 23441081 DOI: 10.1002/Iub.1144 |
0.73 |
|
| 2013 |
Daubner SC, Avila A, Bailey JO, Barrera D, Bermudez JY, Giles DH, Khan CA, Shaheen N, Thompson JW, Vasquez J, Oxley SP, Fitzpatrick PF. Mutagenesis of a specificity-determining residue in tyrosine hydroxylase establishes that the enzyme is a robust phenylalanine hydroxylase but a fragile tyrosine hydroxylase. Biochemistry. 52: 1446-55. PMID 23368961 DOI: 10.1021/Bi400031N |
0.83 |
|
| 2013 |
Roberts KM, Pavon JA, Fitzpatrick PF. Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments. Biochemistry. 52: 1062-73. PMID 23327364 DOI: 10.1021/Bi301675E |
0.812 |
|
| 2012 |
Adachi MS, Taylor AB, Hart PJ, Fitzpatrick PF. Mechanistic and structural analyses of the roles of active site residues in yeast polyamine oxidase Fms1: characterization of the N195A and D94N enzymes. Biochemistry. 51: 8690-7. PMID 23034052 DOI: 10.1021/Bi3011434 |
0.526 |
|
| 2012 |
Tormos JR, Henderson Pozzi M, Fitzpatrick PF. Mechanistic studies of the role of a conserved histidine in a mammalian polyamine oxidase. Archives of Biochemistry and Biophysics. 528: 45-9. PMID 22959971 DOI: 10.1016/J.Abb.2012.08.007 |
0.495 |
|
| 2012 |
Gaweska HM, Roberts KM, Fitzpatrick PF. Isotope effects suggest a stepwise mechanism for berberine bridge enzyme. Biochemistry. 51: 7342-7. PMID 22931234 DOI: 10.1021/Bi300887M |
0.761 |
|
| 2012 |
Adachi MS, Taylor AB, Hart PJ, Fitzpatrick PF. Mechanistic and structural analyses of the role of His67 in the yeast polyamine oxidase Fms1. Biochemistry. 51: 4888-97. PMID 22642831 DOI: 10.1021/Bi300517S |
0.486 |
|
| 2012 |
Fitzpatrick PF. Allosteric regulation of phenylalanine hydroxylase. Archives of Biochemistry and Biophysics. 519: 194-201. PMID 22005392 DOI: 10.1016/J.Abb.2011.09.012 |
0.432 |
|
| 2011 |
Gaweska H, Fitzpatrick PF. Structures and Mechanism of the Monoamine Oxidase Family. Biomolecular Concepts. 2: 365-377. PMID 22022344 DOI: 10.1515/Bmc.2011.030 |
0.427 |
|
| 2011 |
Wang S, Lasagna M, Daubner SC, Reinhart GD, Fitzpatrick PF. Fluorescence spectroscopy as a probe of the effect of phosphorylation at serine 40 of tyrosine hydroxylase on the conformation of its regulatory domain. Biochemistry. 50: 2364-70. PMID 21302933 DOI: 10.1021/Bi101844P |
0.7 |
|
| 2011 |
Panay AJ, Lee M, Krebs C, Bollinger JM, Fitzpatrick PF. Evidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylase. Biochemistry. 50: 1928-33. PMID 21261288 DOI: 10.1021/Bi1019868 |
0.389 |
|
| 2011 |
Li J, Ilangovan U, Daubner SC, Hinck AP, Fitzpatrick PF. Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase. Archives of Biochemistry and Biophysics. 505: 250-5. PMID 20951114 DOI: 10.1016/J.Abb.2010.10.009 |
0.459 |
|
| 2010 |
Adachi MS, Torres JM, Fitzpatrick PF. Mechanistic studies of the yeast polyamine oxidase Fms1: kinetic mechanism, substrate specificity, and pH dependence. Biochemistry. 49: 10440-8. PMID 21067138 DOI: 10.1021/Bi1016099 |
0.46 |
|
| 2010 |
Pavon JA, Eser B, Huynh MT, Fitzpatrick PF. Single turnover kinetics of tryptophan hydroxylase: evidence for a new intermediate in the reaction of the aromatic amino acid hydroxylases. Biochemistry. 49: 7563-71. PMID 20687613 DOI: 10.1021/Bi100744R |
0.796 |
|
| 2010 |
Tormos JR, Taylor AB, Daubner SC, Hart PJ, Fitzpatrick PF. Identification of a hypothetical protein from Podospora anserina as a nitroalkane oxidase. Biochemistry. 49: 5035-41. PMID 20481475 DOI: 10.1021/Bi100610E |
0.48 |
|
| 2010 |
Henderson Pozzi M, Fitzpatrick PF. A lysine conserved in the monoamine oxidase family is involved in oxidation of the reduced flavin in mouse polyamine oxidase. Archives of Biochemistry and Biophysics. 498: 83-8. PMID 20417173 DOI: 10.1016/J.Abb.2010.04.015 |
0.482 |
|
| 2010 |
Panay AJ, Fitzpatrick PF. Measurement of the intramolecular isotope effect on aliphatic hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase. Journal of the American Chemical Society. 132: 5584-5. PMID 20355730 DOI: 10.1021/Ja101563T |
0.436 |
|
| 2010 |
Li J, Dangott LJ, Fitzpatrick PF. Regulation of phenylalanine hydroxylase: conformational changes upon phenylalanine binding detected by hydrogen/deuterium exchange and mass spectrometry. Biochemistry. 49: 3327-35. PMID 20307070 DOI: 10.1021/Bi1001294 |
0.441 |
|
| 2010 |
Valley MP, Fenny NS, Ali SR, Fitzpatrick PF. Characterization of active site residues of nitroalkane oxidase. Bioorganic Chemistry. 38: 115-9. PMID 20056514 DOI: 10.1016/J.Bioorg.2009.12.004 |
0.518 |
|
| 2010 |
Eser BE, Fitzpatrick PF. Measurement of intrinsic rate constants in the tyrosine hydroxylase reaction. Biochemistry. 49: 645-52. PMID 20025246 DOI: 10.1021/Bi901874E |
0.395 |
|
| 2010 |
Adachi MS, Juarez PR, Fitzpatrick PF. Mechanistic studies of human spermine oxidase: kinetic mechanism and pH effects. Biochemistry. 49: 386-92. PMID 20000632 DOI: 10.1021/Bi9017945 |
0.444 |
|
| 2010 |
Fitzpatrick PF. Oxidation of amines by flavoproteins. Archives of Biochemistry and Biophysics. 493: 13-25. PMID 19651103 DOI: 10.1016/J.Abb.2009.07.019 |
0.332 |
|
| 2009 |
Major DT, Heroux A, Orville AM, Valley MP, Fitzpatrick PF, Gao J. Differential quantum tunneling contributions in nitroalkane oxidase catalyzed and the uncatalyzed proton transfer reaction. Proceedings of the National Academy of Sciences of the United States of America. 106: 20734-9. PMID 19926855 DOI: 10.1073/Pnas.0911416106 |
0.389 |
|
| 2009 |
Pozzi MH, Gawandi V, Fitzpatrick PF. Mechanistic studies of para-substituted N,N'-dibenzyl-1,4-diaminobutanes as substrates for a mammalian polyamine oxidase. Biochemistry. 48: 12305-13. PMID 19911805 DOI: 10.1021/Bi901694S |
0.792 |
|
| 2009 |
Chow MS, Eser BE, Wilson SA, Hodgson KO, Hedman B, Fitzpatrick PF, Solomon EI. Spectroscopy and kinetics of wild-type and mutant tyrosine hydroxylase: mechanistic insight into O2 activation. Journal of the American Chemical Society. 131: 7685-98. PMID 19489646 DOI: 10.1021/Ja810080C |
0.371 |
|
| 2009 |
Gaweska H, Henderson Pozzi M, Schmidt DM, McCafferty DG, Fitzpatrick PF. Use of pH and kinetic isotope effects to establish chemistry as rate-limiting in oxidation of a peptide substrate by LSD1. Biochemistry. 48: 5440-5. PMID 19408960 DOI: 10.1021/Bi900499W |
0.419 |
|
| 2009 |
Wang S, Sura GR, Dangott LJ, Fitzpatrick PF. Identification by hydrogen/deuterium exchange of structural changes in tyrosine hydroxylase associated with regulation. Biochemistry. 48: 4972-9. PMID 19371093 DOI: 10.1021/Bi9004254 |
0.797 |
|
| 2009 |
Pavon JA, Fitzpatrick PF. Demonstration of a peroxide shunt in the tetrahydropterin-dependent aromatic amino acid monooxygenases. Journal of the American Chemical Society. 131: 4582-3. PMID 19281164 DOI: 10.1021/Ja900128M |
0.819 |
|
| 2009 |
Héroux A, Bozinovski DM, Valley MP, Fitzpatrick PF, Orville AM. Crystal structures of intermediates in the nitroalkane oxidase reaction. Biochemistry. 48: 3407-16. PMID 19265437 DOI: 10.1021/Bi8023042 |
0.461 |
|
| 2009 |
Henderson Pozzi M, Gawandi V, Fitzpatrick PF. pH dependence of a mammalian polyamine oxidase: insights into substrate specificity and the role of lysine 315. Biochemistry. 48: 1508-16. PMID 19199575 DOI: 10.1021/Bi802227M |
0.426 |
|
| 2008 |
Sarkissian CN, Gámez A, Wang L, Charbonneau M, Fitzpatrick P, Lemontt JF, Zhao B, Vellard M, Bell SM, Henschell C, Lambert A, Tsuruda L, Stevens RC, Scriver CR. Preclinical evaluation of multiple species of PEGylated recombinant phenylalanine ammonia lyase for the treatment of phenylketonuria. Proceedings of the National Academy of Sciences of the United States of America. 105: 20894-9. PMID 19095795 DOI: 10.1073/Pnas.0808421105 |
0.311 |
|
| 2008 |
Panay AJ, Fitzpatrick PF. Kinetic isotope effects on aromatic and benzylic hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase as probes of chemical mechanism and reactivity. Biochemistry. 47: 11118-24. PMID 18817418 DOI: 10.1021/Bi801295W |
0.485 |
|
| 2008 |
Li J, Fitzpatrick PF. Characterization of metal ligand mutants of phenylalanine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad. Archives of Biochemistry and Biophysics. 475: 164-8. PMID 18477464 DOI: 10.1016/J.Abb.2008.04.029 |
0.391 |
|
| 2007 |
Fitzpatrick PF. Insights into the mechanisms of flavoprotein oxidases from kinetic isotope effects. Journal of Labelled Compounds & Radiopharmaceuticals. 50: 1016-1025. PMID 19890477 DOI: 10.1002/Jlcr.1400 |
0.407 |
|
| 2007 |
Fitzpatrick PF, Bozinovski DM, Héroux A, Shaw PG, Valley MP, Orville AM. Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase. Biochemistry. 46: 13800-8. PMID 17994768 DOI: 10.1021/Bi701557K |
0.469 |
|
| 2007 |
Eser BE, Barr EW, Frantom PA, Saleh L, Bollinger JM, Krebs C, Fitzpatrick PF. Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase. Journal of the American Chemical Society. 129: 11334-5. PMID 17715926 DOI: 10.1021/Ja074446S |
0.712 |
|
| 2007 |
Tsai CL, Gokulan K, Sobrado P, Sacchettini JC, Fitzpatrick PF. Mechanistic and structural studies of H373Q flavocytochrome b2: effects of mutating the active site base. Biochemistry. 46: 7844-51. PMID 17563122 DOI: 10.1021/Bi7005543 |
0.72 |
|
| 2007 |
Ralph EC, Hirschi JS, Anderson MA, Cleland WW, Singleton DA, Fitzpatrick PF. Insights into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effects on the reaction of N-methyltryptophan oxidase. Biochemistry. 46: 7655-64. PMID 17542620 DOI: 10.1021/Bi700482H |
0.785 |
|
| 2006 |
Ralph EC, Anderson MA, Cleland WW, Fitzpatrick PF. Mechanistic studies of the flavoenzyme tryptophan 2-monooxygenase: deuterium and 15N kinetic isotope effects on alanine oxidation by an L-amino acid oxidase. Biochemistry. 45: 15844-52. PMID 17176107 DOI: 10.1021/Bi061894O |
0.805 |
|
| 2006 |
Pavon JA, Fitzpatrick PF. Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylation. Biochemistry. 45: 11030-7. PMID 16953590 DOI: 10.1021/Bi0607554 |
0.82 |
|
| 2006 |
Sura GR, Lasagna M, Gawandi V, Reinhart GD, Fitzpatrick PF. Effects of ligands on the mobility of an active-site loop in tyrosine hydroxylase as monitored by fluorescence anisotropy. Biochemistry. 45: 9632-8. PMID 16878998 DOI: 10.1021/Bi060754B |
0.808 |
|
| 2006 |
Daubner SC, McGinnis JT, Gardner M, Kroboth SL, Morris AR, Fitzpatrick PF. A flexible loop in tyrosine hydroxylase controls coupling of amino acid hydroxylation to tetrahydropterin oxidation. Journal of Molecular Biology. 359: 299-307. PMID 16618490 DOI: 10.1016/J.Jmb.2006.03.016 |
0.451 |
|
| 2006 |
Frantom PA, Seravalli J, Ragsdale SW, Fitzpatrick PF. Reduction and oxidation of the active site iron in tyrosine hydroxylase: kinetics and specificity. Biochemistry. 45: 2372-9. PMID 16475826 DOI: 10.1021/Bi052283J |
0.782 |
|
| 2006 |
Nagpal A, Valley MP, Fitzpatrick PF, Orville AM. Crystal structures of nitroalkane oxidase: insights into the reaction mechanism from a covalent complex of the flavoenzyme trapped during turnover. Biochemistry. 45: 1138-50. PMID 16430210 DOI: 10.1021/Bi051966W |
0.414 |
|
| 2006 |
Frantom PA, Seravalli J, Ragsdale SW, Fitzpatrick PF. Erratum: Reduction and oxidation of the active site iron in tyrosine hydroxylase: Kinetics and specificity (Biochemistry (February 21, 2006) 45, 7 (2372-2379)) Biochemistry. 45. DOI: 10.1021/Bi0680072 |
0.726 |
|
| 2005 |
Pavon JA, Fitzpatrick PF. Intrinsic isotope effects on benzylic hydroxylation by the aromatic amino acid hydroxylases: evidence for hydrogen tunneling, coupled motion, and similar reactivities. Journal of the American Chemical Society. 127: 16414-5. PMID 16305226 DOI: 10.1021/Ja0562651 |
0.811 |
|
| 2005 |
Royo M, Fitzpatrick PF. Mechanistic studies of mouse polyamine oxidase with N1,N12-bisethylspermine as a substrate. Biochemistry. 44: 7079-84. PMID 15865452 DOI: 10.1021/Bi050347K |
0.474 |
|
| 2005 |
Ralph EC, Fitzpatrick PF. pH and kinetic isotope effects on sarcosine oxidation by N-methyltryptophan oxidase. Biochemistry. 44: 3074-81. PMID 15723552 DOI: 10.1021/Bi047716H |
0.805 |
|
| 2005 |
Valley MP, Tichy SE, Fitzpatrick PF. Establishing the kinetic competency of the cationic imine intermediate in nitroalkane oxidase. Journal of the American Chemical Society. 127: 2062-6. PMID 15713081 DOI: 10.1021/Ja043542F |
0.458 |
|
| 2005 |
Royo M, Fitzpatrick PF, Daubner SC. Mutation of regulatory serines of rat tyrosine hydroxylase to glutamate: effects on enzyme stability and activity. Archives of Biochemistry and Biophysics. 434: 266-74. PMID 15639226 DOI: 10.1016/J.Abb.2004.11.007 |
0.415 |
|
| 2005 |
Fitzpatrick PF, Orville AM, Nagpal A, Valley MP. Nitroalkane oxidase, a carbanion-forming flavoprotein homologous to acyl-CoA dehydrogenase. Archives of Biochemistry and Biophysics. 433: 157-65. PMID 15581574 DOI: 10.1016/J.Abb.2004.08.021 |
0.483 |
|
| 2005 |
Royo M, Daubner SC, Fitzpatrick PF. Effects of mutations in tyrosine hydroxylase associated with progressive dystonia on the activity and stability of the protein. Proteins. 58: 14-21. PMID 15468323 DOI: 10.1002/Prot.20293 |
0.463 |
|
| 2005 |
Ralph EC, Fitzpatrick PF. Erratum: pH and kinetic isotope effects on sarcosine oxidation by N-methyltryptophan oxidase (Biochemistry (March 1, 2005) 44, 8 (3074-3081)) Biochemistry. 44. DOI: 10.1021/Bi058012Q |
0.773 |
|
| 2005 |
Fitzpatrick P. Special issue on enzyme mechanisms Archives of Biochemistry and Biophysics. 433: 1. DOI: 10.1016/J.Abb.2004.11.001 |
0.392 |
|
| 2004 |
Kansy JW, Daubner SC, Nishi A, Sotogaku N, Lloyd MD, Nguyen C, Lu L, Haycock JW, Hope BT, Fitzpatrick PF, Bibb JA. Identification of tyrosine hydroxylase as a physiological substrate for Cdk5. Journal of Neurochemistry. 91: 374-84. PMID 15447670 DOI: 10.1111/J.1471-4159.2004.02723.X |
0.315 |
|
| 2004 |
Sura GR, Daubner SC, Fitzpatrick PF. Effects of phosphorylation by protein kinase A on binding of catecholamines to the human tyrosine hydroxylase isoforms. Journal of Neurochemistry. 90: 970-8. PMID 15287903 DOI: 10.1111/J.1471-4159.2004.02566.X |
0.794 |
|
| 2004 |
Valley MP, Fitzpatrick PF. Comparison of enzymatic and non-enzymatic nitroethane anion formation: thermodynamics and contribution of tunneling. Journal of the American Chemical Society. 126: 6244-5. PMID 15149217 DOI: 10.1021/Ja0484606 |
0.371 |
|
| 2004 |
Fitzpatrick PF. Carbanion versus hydride transfer mechanisms in flavoprotein-catalyzed dehydrogenations. Bioorganic Chemistry. 32: 125-39. PMID 15110192 DOI: 10.1016/J.Bioorg.2003.02.001 |
0.415 |
|
| 2004 |
Royo M, Daubner SC, Fitzpatrick PF. Specificity of the MAP kinase ERK2 for phosphorylation of tyrosine hydroxylase. Archives of Biochemistry and Biophysics. 423: 247-52. PMID 15001389 DOI: 10.1016/J.Abb.2003.12.027 |
0.384 |
|
| 2003 |
Frantom PA, Fitzpatrick PF. Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical steps. Journal of the American Chemical Society. 125: 16190-1. PMID 14692751 DOI: 10.1021/Ja0383165 |
0.771 |
|
| 2003 |
Sobrado P, Fitzpatrick PF. Solvent and primary deuterium isotope effects show that lactate CH and OH bond cleavages are concerted in Y254F flavocytochrome b2, consistent with a hydride transfer mechanism. Biochemistry. 42: 15208-14. PMID 14690431 DOI: 10.1021/Bi035546N |
0.708 |
|
| 2003 |
Fitzpatrick PF. Mechanism of aromatic amino acid hydroxylation. Biochemistry. 42: 14083-91. PMID 14640675 DOI: 10.1021/Bi035656U |
0.317 |
|
| 2003 |
Sobrado P, Fitzpatrick PF. Identification of Tyr413 as an active site residue in the flavoprotein tryptophan 2-monooxygenase and analysis of its contribution to catalysis. Biochemistry. 42: 13833-8. PMID 14636050 DOI: 10.1021/Bi035300I |
0.742 |
|
| 2003 |
Sobrado P, Fitzpatrick PF. Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member of the L-amino oxidase family. Biochemistry. 42: 13826-32. PMID 14636049 DOI: 10.1021/Bi035299N |
0.726 |
|
| 2003 |
Valley MP, Fitzpatrick PF. Inactivation of nitroalkane oxidase upon mutation of the active site base and rescue with a deprotonated substrate. Journal of the American Chemical Society. 125: 8738-9. PMID 12862464 DOI: 10.1021/Ja036045S |
0.486 |
|
| 2003 |
Valley MP, Fitzpatrick PF. Reductive half-reaction of nitroalkane oxidase: effect of mutation of the active site aspartate to glutamate. Biochemistry. 42: 5850-6. PMID 12741843 DOI: 10.1021/Bi034061W |
0.459 |
|
| 2003 |
Fitzpatrick PF, Ralph EC, Ellis HR, Willmon OJ, Daubner SC. Characterization of metal ligand mutants of tyrosine hydroxylase: insights into the plasticity of a 2-histidine-1-carboxylate triad. Biochemistry. 42: 2081-8. PMID 12590596 DOI: 10.1021/Bi0271493 |
0.828 |
|
| 2002 |
Ellis HR, McCusker KP, Fitzpatrick PF. Use of a tyrosine hydroxylase mutant enzyme with reduced metal affinity allows detection of activity with cobalt in place of iron. Archives of Biochemistry and Biophysics. 408: 305-7. PMID 12464285 DOI: 10.1016/S0003-9861(02)00568-4 |
0.71 |
|
| 2002 |
Sobrado P, Fitzpatrick PF. Analysis of the roles of amino acid residues in the flavoprotein tryptophan 2-monooxygenase modified by 2-oxo-3-pentynoate: characterization of His338, Cys339, and Cys511 mutant enzymes. Archives of Biochemistry and Biophysics. 402: 24-30. PMID 12051679 DOI: 10.1016/S0003-9861(02)00063-2 |
0.709 |
|
| 2002 |
Frantom PA, Pongdee R, Sulikowski GA, Fitzpatrick PF. Intrinsic deuterium isotope effects on benzylic hydroxylation by tyrosine hydroxylase. Journal of the American Chemical Society. 124: 4202-3. PMID 11960436 DOI: 10.1021/Ja025602S |
0.749 |
|
| 2002 |
Daubner SC, Moran GR, Fitzpatrick PF. Role of tryptophan hydroxylase phe313 in determining substrate specificity. Biochemical and Biophysical Research Communications. 292: 639-41. PMID 11922614 DOI: 10.1006/Bbrc.2002.6719 |
0.705 |
|
| 2002 |
Daubner SC, Gadda G, Valley MP, Fitzpatrick PF. Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily. Proceedings of the National Academy of Sciences of the United States of America. 99: 2702-7. PMID 11867731 DOI: 10.1073/Pnas.052527799 |
0.628 |
|
| 2001 |
McCulloch RI, Daubner SC, Fitzpatrick PF. Effects of substitution at serine 40 of tyrosine hydroxylase on catecholamine binding. Biochemistry. 40: 7273-8. PMID 11401575 DOI: 10.1021/Bi010546D |
0.516 |
|
| 2001 |
Gadda G, Banerjee A, Fleming GS, Fitzpatrick PF. Evidence for an essential arginine in the flavoprotein nitroalkane oxidase. Journal of Enzyme Inhibition. 16: 157-63. PMID 11342284 DOI: 10.1080/14756360109162365 |
0.706 |
|
| 2001 |
Fitzpatrick PF. Substrate dehydrogenation by flavoproteins. Accounts of Chemical Research. 34: 299-307. PMID 11308304 DOI: 10.1021/Ar0000511 |
0.452 |
|
| 2001 |
Sobrado P, Daubner SC, Fitzpatrick PF. Probing the relative timing of hydrogen abstraction steps in the flavocytochrome b2 reaction with primary and solvent deuterium isotope effects and mutant enzymes. Biochemistry. 40: 994-1001. PMID 11170421 DOI: 10.1021/Bi002283D |
0.713 |
|
| 2000 |
Gadda G, Choe DY, Fitzpatrick PF. Use of pH and kinetic isotope effects to dissect the effects of substrate size on binding and catalysis by nitroalkane oxidase. Archives of Biochemistry and Biophysics. 382: 138-44. PMID 11051107 DOI: 10.1006/Abbi.2000.2009 |
0.647 |
|
| 2000 |
Daubner SC, Melendez J, Fitzpatrick PF. Reversing the substrate specificities of phenylalanine and tyrosine hydroxylase: aspartate 425 of tyrosine hydroxylase is essential for L-DOPA formation. Biochemistry. 39: 9652-61. PMID 10933781 DOI: 10.1021/Bi000493K |
0.474 |
|
| 2000 |
Gadda G, Banerjee A, Dangott LJ, Fitzpatrick PF. Identification of a cysteine residue in the active site of nitroalkane oxidase by modification with N-ethylmaleimide. The Journal of Biological Chemistry. 275: 31891-5. PMID 10913134 DOI: 10.1074/Jbc.M003679200 |
0.68 |
|
| 2000 |
Fitzpatrick PF. The aromatic amino acid hydroxylases. Advances in Enzymology and Related Areas of Molecular Biology. 74: 235-94. PMID 10800597 DOI: 10.1002/9780470123201.Ch6 |
0.518 |
|
| 2000 |
Ellis HR, Daubner SC, Fitzpatrick PF. Mutation of serine 395 of tyrosine hydroxylase decouples oxygen-oxygen bond cleavage and tyrosine hydroxylation. Biochemistry. 39: 4174-81. PMID 10747809 DOI: 10.1021/Bi9928546 |
0.769 |
|
| 2000 |
Gadda G, Fitzpatrick PF. Mechanism of nitroalkane oxidase: 2. pH and kinetic isotope effects. Biochemistry. 39: 1406-10. PMID 10684621 DOI: 10.1021/Bi992255Z |
0.625 |
|
| 2000 |
Gadda G, Fitzpatrick PF. Iso-mechanism of nitroalkane oxidase: 1. Inhibition studies and activation by imidazole. Biochemistry. 39: 1400-5. PMID 10684620 DOI: 10.1021/Bi9922547 |
0.685 |
|
| 2000 |
Gadda G, Banerjee A, Fitzpatrick PF. Identification of an essential tyrosine residue in nitroalkane oxidase by modification with tetranitromethane. Biochemistry. 39: 1162-8. PMID 10653664 DOI: 10.1021/Bi9921743 |
0.699 |
|
| 2000 |
Ramsey AJ, Fitzpatrick PF. Effects of phosphorylation on binding of catecholamines to tyrosine hydroxylase: specificity and thermodynamics. Biochemistry. 39: 773-8. PMID 10651643 DOI: 10.1021/Bi991901R |
0.425 |
|
| 2000 |
Moran GR, Derecskei-Kovacs A, Hillas PJ, Fitzpatrick PF. On the catalytic mechanism of tryptophan hydroxylase Journal of the American Chemical Society. 122: 4535-4541. DOI: 10.1021/Ja994479A |
0.632 |
|
| 2000 |
Kurtz KA, Rishavy MA, Cleland WW, Fitzpatrick PF. Nitrogen isotope effects as probes of the mechanism of D-amino acid oxidase [17] Journal of the American Chemical Society. 122: 12896-12897. DOI: 10.1021/Ja002528+ |
0.327 |
|
| 1999 |
Fitzpatrick PF. Tetrahydropterin-dependent amino acid hydroxylases. Annual Review of Biochemistry. 68: 355-81. PMID 10872454 DOI: 10.1146/Annurev.Biochem.68.1.355 |
0.483 |
|
| 1999 |
Simonian AL, Rainina EI, Fitzpatrick PF, Wild J. Enhancement of the specificity of an enzyme-based biosensor for L-tryptophan. Advances in Experimental Medicine and Biology. 467: 833-40. PMID 10721137 DOI: 10.1007/978-1-4615-4709-9_106 |
0.336 |
|
| 1999 |
Moran GR, Phillips RS, Fitzpatrick PF. Influence of steric bulk and electrostatics on the hydroxylation regiospecificity of tryptophan hydroxylase: characterization of methyltryptophans and azatryptophans as substrates. Biochemistry. 38: 16283-9. PMID 10587452 DOI: 10.1021/Bi991983J |
0.677 |
|
| 1999 |
Ellis HR, Daubner SC, McCulloch RI, Fitzpatrick PF. Phenylalanine residues in the active site of tyrosine hydroxylase: mutagenesis of Phe300 and Phe309 to alanine and metal ion-catalyzed hydroxylation of Phe300. Biochemistry. 38: 10909-14. PMID 10460145 DOI: 10.1021/Bi991160U |
0.764 |
|
| 1999 |
McCulloch RI, Fitzpatrick PF. Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conformationally sensitive to phosphorylation state and dopamine binding. Archives of Biochemistry and Biophysics. 367: 143-5. PMID 10375411 DOI: 10.1006/Abbi.1999.1259 |
0.329 |
|
| 1999 |
Gadda G, Dangott LJ, Johnson WH, Whitman CP, Fitzpatrick PF. Characterization of 2-oxo-3-pentynoate as an active-site-directed inactivator of flavoprotein oxidases: identification of active-site peptides in tryptophan 2-monooxygenase. Biochemistry. 38: 5822-8. PMID 10231533 DOI: 10.1021/Bi982777Z |
0.677 |
|
| 1999 |
Daubner SC, Fitzpatrick PF. Site-directed mutants of charged residues in the active site of tyrosine hydroxylase. Biochemistry. 38: 4448-54. PMID 10194366 DOI: 10.1021/Bi983012U |
0.484 |
|
| 1999 |
Gadda G, Fitzpatrick PF. Substrate specificity of a nitroalkane-oxidizing enzyme. Archives of Biochemistry and Biophysics. 363: 309-13. PMID 10068453 DOI: 10.1006/Abbi.1998.1081 |
0.688 |
|
| 1999 |
Moran GR, Fitzpatrick PF. A continuous fluorescence assay for tryptophan hydroxylase. Analytical Biochemistry. 266: 148-52. PMID 9887224 DOI: 10.1006/Abio.1998.2956 |
0.629 |
|
| 1998 |
Daubner SC, Fitzpatrick PF. Mutation to phenylalanine of tyrosine 371 in tyrosine hydroxylase increases the affinity for phenylalanine. Biochemistry. 37: 16440-4. PMID 9819237 DOI: 10.1021/Bi981648F |
0.519 |
|
| 1998 |
Ramsey AJ, Fitzpatrick PF. Effects of phosphorylation of serine 40 of tyrosine hydroxylase on binding of catecholamines: evidence for a novel regulatory mechanism. Biochemistry. 37: 8980-6. PMID 9636040 DOI: 10.1021/Bi980582L |
0.445 |
|
| 1998 |
Moran GR, Daubner SC, Fitzpatrick PF. Expression and characterization of the catalytic core of tryptophan hydroxylase. The Journal of Biological Chemistry. 273: 12259-66. PMID 9575176 DOI: 10.1074/Jbc.273.20.12259 |
0.654 |
|
| 1998 |
Gadda G, Fitzpatrick PF. Biochemical and physical characterization of the active FAD-containing form of nitroalkane oxidase from Fusarium oxysporum. Biochemistry. 37: 6154-64. PMID 9558355 DOI: 10.1021/Bi973085Y |
0.703 |
|
| 1998 |
Francisco WA, Tian G, Fitzpatrick PF, Klinman JP. Oxygen-18 kinetic isotope effect studies of the tyrosine hydroxylase reaction: Evidence of rate limiting oxygen activation Journal of the American Chemical Society. 120: 4057-4062. DOI: 10.1021/Ja973543Q |
0.416 |
|
| 1997 |
Daubner SC, Hillas PJ, Fitzpatrick PF. Expression and characterization of the catalytic domain of human phenylalanine hydroxylase. Archives of Biochemistry and Biophysics. 348: 295-302. PMID 9434741 DOI: 10.1006/Abbi.1997.0435 |
0.491 |
|
| 1997 |
Daubner SC, Hillas PJ, Fitzpatrick PF. Characterization of chimeric pterin-dependent hydroxylases: contributions of the regulatory domains of tyrosine and phenylalanine hydroxylase to substrate specificity. Biochemistry. 36: 11574-82. PMID 9305947 DOI: 10.1021/Bi9711137 |
0.422 |
|
| 1997 |
Goodwill KE, Sabatier C, Marks C, Raag R, Fitzpatrick PF, Stevens RC. Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases. Nature Structural Biology. 4: 578-85. PMID 9228951 DOI: 10.1038/Nsb0797-578 |
0.401 |
|
| 1997 |
Gadda G, Edmondson RD, Russell DH, Fitzpatrick PF. Identification of the naturally occurring flavin of nitroalkane oxidase from fusarium oxysporum as a 5-nitrobutyl-FAD and conversion of the enzyme to the active FAD-containing form. The Journal of Biological Chemistry. 272: 5563-70. PMID 9038163 DOI: 10.1074/Jbc.272.9.5563 |
0.668 |
|
| 1997 |
Kurtz KA, Fitzpatrick PF. pH and secondary kinetic isotope effects on the reaction of D-amino acid oxidase with nitroalkane anions: Evidence for direct attack on the flavin by carbanions Journal of the American Chemical Society. 119: 1155-1156. DOI: 10.1021/Ja962783N |
0.377 |
|
| 1997 |
Edmondson RD, Gadda G, Fitzpatrick PF, Russell DH. Identification of Native Flavin Adducts Fusarium oxysporum Using Accurate Mass Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry Analytical Chemistry. 69: 2862-2865. DOI: 10.1021/Ac9700989 |
0.527 |
|
| 1997 |
Fitzpatrick PF, Kurtz KA, Denu JM, Emanuele JF. Contrasting values of commitment factors measured from viscosity, pH, and kinetic isotope effects: Evidence for slow conformational changes in the D-amino acid oxidase reaction Bioorganic Chemistry. 25: 100-109. DOI: 10.1006/Bioo.1997.1057 |
0.641 |
|
| 1996 |
Ramsey AJ, Hillas PJ, Fitzpatrick PF. Characterization of the active site iron in tyrosine hydroxylase. Redox states of the iron. The Journal of Biological Chemistry. 271: 24395-400. PMID 8798695 DOI: 10.1074/Jbc.271.40.24395 |
0.378 |
|
| 1996 |
Heasley CJ, Fitzpatrick PF. Kinetic mechanism and substrate specificity of nitroalkane oxidase. Biochemical and Biophysical Research Communications. 225: 6-10. PMID 8769086 DOI: 10.1006/Bbrc.1996.1122 |
0.499 |
|
| 1996 |
Hillas PJ, Fitzpatrick PF. A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines. Biochemistry. 35: 6969-75. PMID 8679520 DOI: 10.1021/Bi9606861 |
0.401 |
|
| 1995 |
Ramsey AJ, Daubner SC, Ehrlich JI, Fitzpatrick PF. Identification of iron ligands in tyrosine hydroxylase by mutagenesis of conserved histidinyl residues. Protein Science : a Publication of the Protein Society. 4: 2082-6. PMID 8535244 DOI: 10.1002/Pro.5560041013 |
0.451 |
|
| 1995 |
Emanuele JJ, Fitzpatrick PF. Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 2. pH and kinetic isotope effects. Biochemistry. 34: 3716-23. PMID 7893668 DOI: 10.1021/Bi00011A029 |
0.432 |
|
| 1995 |
Emanuele JJ, Fitzpatrick PF. Mechanistic studies of the flavoprotein tryptophan 2-monooxygenase. 1. Kinetic mechanism. Biochemistry. 34: 3710-5. PMID 7893667 DOI: 10.1021/Bi00011A028 |
0.438 |
|
| 1995 |
Emanuele JJ, Heasley CJ, Fitzpatrick PF. Purification and characterization of the flavoprotein tryptophan 2-monooxygenase expressed at high levels in Escherichia coli. Archives of Biochemistry and Biophysics. 316: 241-8. PMID 7840624 DOI: 10.1006/Abbi.1995.1034 |
0.493 |
|
| 1994 |
Kulathila R, Consalvo AP, Fitzpatrick PF, Freeman JC, Snyder LM, Villafranca JJ, Merkler DJ. Bifunctional peptidylglcine alpha-amidating enzyme requires two copper atoms for maximum activity. Archives of Biochemistry and Biophysics. 311: 191-5. PMID 8185317 DOI: 10.1006/Abbi.1994.1225 |
0.618 |
|
| 1994 |
Denu JM, Fitzpatrick PF. pH and kinetic isotope effects on the oxidative half-reaction of D-amino-acid oxidase. The Journal of Biological Chemistry. 269: 15054-9. PMID 7910822 |
0.594 |
|
| 1994 |
Denu JM, Fitzpatrick PF. Intrinsic primary, secondary, and solvent kinetic isotope effects on the reductive half-reaction of D-amino acid oxidase: evidence against a concerted mechanism. Biochemistry. 33: 4001-7. PMID 7908225 DOI: 10.1021/Bi00179A029 |
0.631 |
|
| 1994 |
Fitzpatrick PF. Kinetic isotope effects on hydroxylation of ring-deuterated phenylalanines by tyrosine hydroxylase provide evidence against partitioning of an arene oxide intermediate Journal of the American Chemical Society. 116: 1133-1134. DOI: 10.1021/Ja00082A046 |
0.357 |
|
| 1993 |
Daubner SC, Lohse DL, Fitzpatrick PF. Expression and characterization of catalytic and regulatory domains of rat tyrosine hydroxylase. Protein Science : a Publication of the Protein Society. 2: 1452-60. PMID 8104613 DOI: 10.1002/Pro.5560020909 |
0.412 |
|
| 1993 |
Daubner SC, Fitzpatrick PF. Lysine241 of Tyrosine Hydroxylase Is Not Required for Binding of Tetrahydrobiopterin Substrate Archives of Biochemistry and Biophysics. 302: 455-460. PMID 8098196 DOI: 10.1006/Abbi.1993.1239 |
0.49 |
|
| 1993 |
Daubner SC, Fitzpatrick PF. Alleviation of catecholamine inhibition of tyrosine hydroxylase by phosphorylation at serine40 Advances in Experimental Medicine and Biology. 338: 87-92. PMID 7905703 DOI: 10.1007/978-1-4615-2960-6_17 |
0.413 |
|
| 1993 |
Fitzpatrick PF. Mechanistic studies of tyrosine hydroxylase Advances in Experimental Medicine and Biology. 338: 81-86. PMID 7905702 DOI: 10.1007/978-1-4615-2960-6_16 |
0.417 |
|
| 1993 |
Lohse DL, Fitzpatrick PF. Identification of the intersubunit binding region in rat tyrosine hydroxylase. Biochemical and Biophysical Research Communications. 197: 1543-8. PMID 7904160 DOI: 10.1006/Bbrc.1993.2653 |
0.385 |
|
| 1992 |
Meyer MM, Fitzpatrick PF. The amino acid substrate of bovine tyrosine hydroxylase. Neurochemistry International. 21: 191-6. PMID 1363863 DOI: 10.1016/0197-0186(92)90146-I |
0.462 |
|
| 1992 |
Denu JM, Fitzpatrick PF. pH and kinetic isotope effects on the reductive half-reaction of D-amino acid oxidase. Biochemistry. 31: 8207-15. PMID 1356021 DOI: 10.1021/Bi00150A013 |
0.619 |
|
| 1992 |
Daubner SC, Lauriano C, Haycock JW, Fitzpatrick PF. Site-directed mutagenesis of serine 40 of rat tyrosine hydroxylase: Effects of dopamine and cAMP-dependent phosphorylation on enzyme activity Journal of Biological Chemistry. 267: 12639-12646. PMID 1352289 |
0.393 |
|
| 1991 |
Fitzpatrick PF. Studies of the rate-limiting step in the tyrosine hydroxylase reaction: Alternate substrates, solvent isotope effects, and transition-state analogues Biochemistry. 30: 6386-6391. PMID 1675871 DOI: 10.1021/Bi00240A006 |
0.447 |
|
| 1991 |
Fitzpatrick PF. Steady-state kinetic mechanism of rat tyrosine hydroxylase Biochemistry. 30: 3658-3662. PMID 1673058 DOI: 10.1021/Bi00229A010 |
0.423 |
|
| 1990 |
Robertson JG, Desai PR, Kumar A, Farrington GK, Fitzpatrick PF, Villafranca JJ. Primary amino acid sequence of bovine dopamine beta-hydroxylase. The Journal of Biological Chemistry. 265: 1029-35. PMID 2295597 |
0.545 |
|
| 1989 |
Fitzpatrick PF. The metal requirement of rat tyrosine hydroxylase Biochemical and Biophysical Research Communications. 161: 211-215. PMID 2567163 DOI: 10.1016/0006-291X(89)91582-9 |
0.341 |
|
| 1988 |
Fitzpatrick PF. The pH dependence of binding of inhibitors to bovine adrenal tyrosine hydroxylase Journal of Biological Chemistry. 263: 16058-16062. PMID 2903149 |
0.355 |
|
| 1987 |
Fitzpatrick PF, Villafranca JJ. Mechanism-based inhibitors of dopamine beta-hydroxylase. Archives of Biochemistry and Biophysics. 257: 231-50. PMID 3662525 DOI: 10.1016/0003-9861(87)90563-7 |
0.591 |
|
| 1986 |
Fitzpatrick PF, Harpel MR, Villafranca JJ. Use of alternate substrates to probe the order of substrate addition to dopamine beta-hydroxylase. Archives of Biochemistry and Biophysics. 249: 70-5. PMID 3740855 DOI: 10.1016/0003-9861(86)90561-8 |
0.655 |
|
| 1986 |
Fitzpatrick PF, Villafranca JJ. The mechanism of inactivation of dopamine beta-hydroxylase by hydrazines. The Journal of Biological Chemistry. 261: 4510-8. PMID 3007460 |
0.6 |
|
| 1985 |
Fitzpatrick PF, Flory DR, Villafranca JJ. 3-Phenylpropenes as mechanism-based inhibitors of dopamine beta-hydroxylase: evidence for a radical mechanism. Biochemistry. 24: 2108-14. PMID 3995005 DOI: 10.1021/Bi00330A003 |
0.622 |
|
| 1985 |
Fitzpatrick PF, Ghisla S, Massey V. 8-Azidoflavins as photoaffinity labels for flavoproteins. The Journal of Biological Chemistry. 260: 8483-91. PMID 2861204 |
0.534 |
|
| 1985 |
Fitzpatrick PF, Villafranca JJ. Mechanism-based inhibitors of dopamine β-hydroxylase containing acetylenic or cyclopropyl groups Journal of the American Chemical Society. 107: 5022-5023. DOI: 10.1002/Chin.198549099 |
0.547 |
|
| 1985 |
Fitzpatrick PF, Villafranca JJ. Mechanism-based inhibitors for dopamine β-hydroxylase containing vinyl, acetylenic, or cyclopropyl substituents: Evidence for a radical mechanism Federation Proceedings. 44: No. 5777. |
0.509 |
|
| 1984 |
Rajashekhar B, Fitzpatrick PF, Colombo G, Villafranca JJ. Synthesis of several 2-substituted 3-(p-hydroxyphenyl)-1-propenes and their characterization as mechanism-based inhibitors of dopamine beta-hydroxylase. The Journal of Biological Chemistry. 259: 6925-30. PMID 6547138 |
0.577 |
|
| 1983 |
Fitzpatrick PF, Massey V. The reaction of 8-mercaptoflavins and flavoproteins with sulfite. Evidence for the role of an active site arginine in D-amino acid oxidase. The Journal of Biological Chemistry. 258: 9700-5. PMID 6136504 |
0.551 |
|
| 1982 |
Claiborne A, Massey V, Fitzpatrick PF, Schopfer LM. 2-Thioflavins as active site probes of flavoproteins. The Journal of Biological Chemistry. 257: 174-82. PMID 7053365 |
0.465 |
|
| 1982 |
Fitzpatrick PF, Massey V. The kinetic mechanism of D-amino acid oxidase with D-alpha-aminobutyrate as substrate. Effect of enzyme concentration on the kinetics. The Journal of Biological Chemistry. 257: 12916-23. PMID 6127341 |
0.563 |
|
| 1982 |
Fitzpatrick PF, Massey V. Proton release during the reductive half-reaction of D-amino acid oxidase. The Journal of Biological Chemistry. 257: 9958-62. PMID 6125513 |
0.561 |
|
| 1982 |
Fitzpatrick PF, Massey V. Thiazolidine-2-carboxylic acid, an adduct of cysteamine and glyoxylate, as a substrate for D-amino acid oxidase. The Journal of Biological Chemistry. 257: 1166-71. PMID 6120164 |
0.552 |
|
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