Kinetic Mechanism and Intrinsic Rate Constants for the Reaction of a Bacterial Phenylalanine Hydroxylase
Author:
Affiliation:
1. Department of Biochemistry, University of Texas Health Science Center at San Antonio, San Antonio Texas 78229, United States
Funder
Division of Chemistry
Welch Foundation
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.6b01012
Reference35 articles.
1. Tetrahydropterin-Dependent Amino Acid Hydroxylases
2. Three-Dimensional Structure of Human Tryptophan Hydroxylase and Its Implications for the Biosynthesis of the Neurotransmitters Serotonin and Melatonin,
3. Structural Comparison of Bacterial and Human Iron-dependent Phenylalanine Hydroxylases: Similar Fold, Different Stability and Reaction Rates
4. 2.0Å Resolution Crystal Structures of the Ternary Complexes of Human Phenylalanine Hydroxylase Catalytic Domain with Tetrahydrobiopterin and 3-(2-Thienyl)-l-alanine or l-Norleucine: Substrate Specificity and Molecular Motions Related to Substrate Binding
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1. Biochemical and biophysical approaches to characterization of the aromatic amino acid hydroxylases;Methods in Enzymology;2024
2. The aromatic amino acid hydroxylases: Structures, catalysis, and regulation of phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase;Archives of Biochemistry and Biophysics;2023-02
3. How Do Preorganized Electric Fields Function in Catalytic Cycles? The Case of the Enzyme Tyrosine Hydroxylase;Journal of the American Chemical Society;2022-10-25
4. Thermodynamics of iron, tetrahydrobiopterin, and phenylalanine binding to phenylalanine hydroxylase from Chromobacterium violaceum;Archives of Biochemistry and Biophysics;2022-10
5. Structural studies of a novel auxiliary-domain-containing phenylalanine hydroxylase from Bacillus cereus ATCC 14579;Acta Crystallographica Section D Structural Biology;2022-04-08
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