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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
Establishing the kinetic competency of the cationic imine intermediate in nitroalkane oxidase.
TL;DR: The present results are consistent with cyanide trapping this electrophilic intermediate and removal of a proton from the nitroalkane, forming a carbanion which adds to the flavin N(5).
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Use of pH and kinetic isotope effects to establish chemistry as rate-limiting in oxidation of a peptide substrate by LSD1.
Helena Gaweska,Michelle Henderson Pozzi,Dawn M. Z. Schmidt,Dewey G. McCafferty,Paul F. Fitzpatrick +4 more
TL;DR: The mechanism of oxidation of a peptide substrate by the flavoprotein lysine-specific demethylase (LSD1) has been examined using the effects of pH and isotopic substitution on steady-state and rapid-reaction kinetic parameters.
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Kinetic Mechanism and Substrate Specificity of Nitroalkane Oxidase
TL;DR: The pH dependences of the V/K values for 1-nitropentane and phenylnitromethane show that an amino acid residue on the enzyme with a pKa-value of 6.7 must be unprotonated for activity with both substrates, establishing that the nitroalkane must be in the neutral rather than the anionic form for catalysis.
Journal ArticleDOI
Substrate specificity of a nitroalkane-oxidizing enzyme.
TL;DR: The substrate specificity of the FAD-containing enzyme has been determined as a probe of the active site structure, suggesting a hydrophobic binding site sufficient to accommodate a four carbon chain in nitroalkane oxidase.
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Effects of substitution at serine 40 of tyrosine hydroxylase on catecholamine binding.
TL;DR: The results suggest that the serine hydroxyl contributes to the stabilization of the catecholamine-inhibited enzyme, and the S40E enzyme will be useful in further studies of the effects of multiple phosphorylation on tyrosines, while the alanine enzyme does not provide an accurate mimic of the unphosphorylated enzyme.