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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
Mechanism of the Flavoprotein d-6-Hydroxynicotine Oxidase: Substrate Specificity, pH and Solvent Isotope Effects, and Roles of Key Active-Site Residues.
Paul F. Fitzpatrick,Vi Dougherty,Bishnu P. Subedi,Jesus Quilantan,Cynthia S. Hinck,Andreina I. Lujan,José R. Tormos +6 more
TL;DR: The results are consistent with a network of hydrogen-bonded residues in the active site being involved in binding the neutral form of theAmine substrate, followed by the transfer of a hydride from the amine to the flavin.
Book ChapterDOI
Enhancement of the specificity of an enzyme-based biosensor for L-tryptophan
TL;DR: A new selective amperometric biosensor for reagentless L-tryptophan determination has been developed using immobilized tryptophan-2-monooxygenase (TMO, EC 1.13.12.3), which retained catalytic activity and fidelity of phenylalanine and tryPTophan response for greater than 4 months with repeated usage.
Journal ArticleDOI
Identification of the rate-limiting step in serine proteinases from the effect of temperature on steady-state kinetics
TL;DR: The temperature dependence of the steady-state kinetic parameters of t-Boc-Ala-AlA-Pro-ala p-nitroanilide and N-acetyl-Alo- Ala-alpha-Aza-Alas p-Nitrophenyl ester have been determined and are consistent with the prediction that acylation is rate-limiting.
Journal ArticleDOI
pH and deuterium isotope effects on the reaction of trimethylamine dehydrogenase with dimethylamine.
TL;DR: P pH and kinetic isotope effects with the slow substrate dimethylamine to study the mechanism of amine oxidation suggest the presence of an alternative pathway at low pH, in which the protonated substrate binds and is then deprotonated by an active-site residue prior to oxidation.
Book ChapterDOI
Measurement of Kinetic Isotope Effects in an Enzyme-Catalyzed Reaction by Continuous-Flow Mass Spectrometry.
TL;DR: The use of continuous-flow mass spectrometry is described to determine the deuterium KIE for the enzyme N-acetylpolyamine oxidase based on the ratio of labeled and unlabeled products in mass spectra of whole reaction mixtures.