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Paul F. Fitzpatrick
Researcher at University of Texas Health Science Center at San Antonio
Publications - 195
Citations - 7045
Paul F. Fitzpatrick is an academic researcher from University of Texas Health Science Center at San Antonio. The author has contributed to research in topics: Tyrosine hydroxylase & Phenylalanine hydroxylase. The author has an hindex of 42, co-authored 192 publications receiving 6514 citations. Previous affiliations of Paul F. Fitzpatrick include Brookhaven National Laboratory & Texas A&M University.
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Journal ArticleDOI
The Amino Acid Specificity for Activation of Phenylalanine Hydroxylase Matches the Specificity for Stabilization of Regulatory Domain Dimers
TL;DR: The results support a model in which allosteric activation of phenylalanine hydroxylase is linked to dimerization of regulatory domains.
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Kinetic isotope effects on aromatic and benzylic hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase as probes of chemical mechanism and reactivity.
TL;DR: Evidence is provided that the reactivities of the prokaryotic and eukaryotic hydroxylases are similar and the reactivity of the iron center for the family of aromatic amino acid hydroxyases is defined.
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An empirical analysis of enzyme function reporting for experimental reproducibility: Missing/incomplete information in published papers.
Peter J. Halling,Paul F. Fitzpatrick,Frank M. Raushel,Johann M. Rohwer,Santiago Schnell,Ulrike Wittig,Roland Wohlgemuth,Carsten Kettner +7 more
TL;DR: A detailed examination of 11 recent papers (and their supplementary material) from two leading journals found that in every paper they were not able to collect some critical information necessary to reproduce the enzyme function findings.
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Mechanism of the Flavoprotein L-Hydroxynicotine Oxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product, and Roles of Active-Site Residues.
TL;DR: Analysis of the product of the enzyme from Arthrobacter nicotinovorans by nuclear magnetic resonance and continuous-flow mass spectrometry establishes that the enzyme catalyzes the oxidation of the pyrrolidine carbon-nitrogen bond, the expected reaction for a monoamine oxidase, and that hydrolysis of the amine to form 6-hydroxypseudooxynicotine is nonenzymatic.
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Nitroalkane oxidase: Structure and mechanism.
TL;DR: A combination of solution and structural analyses have provided a detailed understanding of the mechanism of this enzyme.