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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 kinetic mechanism of D-amino acid oxidase with D-alpha-aminobutyrate as substrate. Effect of enzyme concentration on the kinetics.
TL;DR: Computer simulations show that the kinetic isotopes effects on the reductive half-reaction with D-alanine reported by Porter et al. can be explained using a two-step model with a kinetic isotope effect of 1.75 on the limiting rate of reduction.
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Reductive half-reaction of nitroalkane oxidase: Effect of mutation of the active site aspartate to glutamate
TL;DR: Results support the assignment of Asp402 as the active site base in nitroalkane oxidase, which is homologous to the acyl-CoA dehydrogenase family of enzymes.
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Mechanism of nitroalkane oxidase: 2. pH and kinetic isotope effects
TL;DR: P pH and kinetic isotope effects with [1, 1-(2)H(2)]nitroethane have been used to study the mechanism of nitroalkane oxidase, indicating that nitroethylene has no significant external commitments to catalysis.
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STRENDA DB: enabling the validation and sharing of enzyme kinetics data.
Neil Swainston,Antonio Baici,Barbara M. Bakker,Athel Cornish-Bowden,Paul F. Fitzpatrick,Peter J. Halling,Thomas S. Leyh,Claire O'Donovan,Frank M. Raushel,Udo Reschel,Johann M. Rohwer,Santiago Schnell,Dietmar Schomburg,Keith F. Tipton,Ming-Daw Tsai,Hans V. Westerhoff,Hans V. Westerhoff,Hans V. Westerhoff,Ulrike Wittig,Roland Wohlgemuth,Carsten Kettner +20 more
TL;DR: STRENDA DB provides authors who are preparing a manuscript with a user-friendly, web-based service that checks automatically enzymology data sets entered in the submission form that they are complete and valid before they are submitted as part of a publication to a journal.
Journal ArticleDOI
Kinetic mechanism of phenylalanine hydroxylase: intrinsic binding and rate constants from single-turnover experiments.
TL;DR: Similar reactions using 6-methyltetrahydropterin indicate a preference for the physiological pterin during hydroxylation in PheH, which largely determines k(cat).