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Paul F Fitzpatrick

Showing results (21-30 of 108) with videos related to

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Biochemistry|November 26, 2003
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member of the L-amino oxidase familyPablo Sobrado, Paul F Fitzpatrick
Biochemistry|November 26, 2003
Identification of Tyr413 as an active site residue in the flavoprotein tryptophan 2-monooxygenase and analysis of its contribution to catalysisPablo Sobrado, Paul F Fitzpatrick
Journal of the American Chemical Society|December 25, 2003
Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical stepsPatrick A Frantom, Paul F Fitzpatrick
Methods in Enzymology|September 20, 2024
Biochemical and biophysical approaches to characterization of the aromatic amino acid hydroxylasesPaul F Fitzpatrick, S Colette Daubner
Biochemistry|September 7, 2006
Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylationJorge Alex Pavon, Paul F Fitzpatrick
IUBMB Life|February 27, 2013
Mechanisms of tryptophan and tyrosine hydroxylaseKenneth M Roberts, Paul F Fitzpatrick
Biochemistry|December 23, 2009
Measurement of intrinsic rate constants in the tyrosine hydroxylase reactionBekir E Eser, Paul F Fitzpatrick
Journal of the American Chemical Society|March 29, 2018
Mutagenesis of an Active-Site Loop in Tryptophan Hydroxylase Dramatically Slows the Formation of an Early Intermediate in CatalysisBishnu P Subedi, Paul F Fitzpatrick
Biochemistry|September 27, 2008
Kinetic isotope effects on aromatic and benzylic hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase as probes of chemical mechanism and reactivityAram J Panay, Paul F Fitzpatrick
Biochemistry|October 23, 2018
Phosphorylation of Phenylalanine Hydroxylase Increases the Rate Constant for Formation of the Activated Conformation of the EnzymeCrystal A Khan, Paul F Fitzpatrick
Pageof 11

Showing results (21-30 of 108) with videos related to

Sort By:
Pageof 11
Biochemistry|November 26, 2003
Analysis of the role of the active site residue Arg98 in the flavoprotein tryptophan 2-monooxygenase, a member of the L-amino oxidase familyPablo Sobrado, Paul F Fitzpatrick
Biochemistry|November 26, 2003
Identification of Tyr413 as an active site residue in the flavoprotein tryptophan 2-monooxygenase and analysis of its contribution to catalysisPablo Sobrado, Paul F Fitzpatrick
Journal of the American Chemical Society|December 25, 2003
Uncoupled forms of tyrosine hydroxylase unmask kinetic isotope effects on chemical stepsPatrick A Frantom, Paul F Fitzpatrick
Methods in Enzymology|September 20, 2024
Biochemical and biophysical approaches to characterization of the aromatic amino acid hydroxylasesPaul F Fitzpatrick, S Colette Daubner
Biochemistry|September 7, 2006
Insights into the catalytic mechanisms of phenylalanine and tryptophan hydroxylase from kinetic isotope effects on aromatic hydroxylationJorge Alex Pavon, Paul F Fitzpatrick
IUBMB Life|February 27, 2013
Mechanisms of tryptophan and tyrosine hydroxylaseKenneth M Roberts, Paul F Fitzpatrick
Biochemistry|December 23, 2009
Measurement of intrinsic rate constants in the tyrosine hydroxylase reactionBekir E Eser, Paul F Fitzpatrick
Journal of the American Chemical Society|March 29, 2018
Mutagenesis of an Active-Site Loop in Tryptophan Hydroxylase Dramatically Slows the Formation of an Early Intermediate in CatalysisBishnu P Subedi, Paul F Fitzpatrick
Biochemistry|September 27, 2008
Kinetic isotope effects on aromatic and benzylic hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase as probes of chemical mechanism and reactivityAram J Panay, Paul F Fitzpatrick
Biochemistry|October 23, 2018
Phosphorylation of Phenylalanine Hydroxylase Increases the Rate Constant for Formation of the Activated Conformation of the EnzymeCrystal A Khan, Paul F Fitzpatrick
Pageof 11