Structural Comparison of Bacterial and Human Iron-dependent Phenylalanine Hydroxylases: Similar Fold, Different Stability and Reaction Rates
- 27 June 2002
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 320 (3), 645-661
- https://doi.org/10.1016/s0022-2836(02)00496-5
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Use of Surface Plasmon Resonance for Real-Time Measurements of the Global Conformational Transition in Human Phenylalanine Hydroxylase in Response to Substrate Binding and Catalytic ActivationAnalytical Biochemistry, 2001
- Crystal Structure and Site-Specific Mutagenesis of Pterin-Bound Human Phenylalanine Hydroxylase,Biochemistry, 2000
- The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: implications for the catalytic mechanismJournal of Molecular Biology, 1999
- Structural Insight into the Aromatic Amino Acid Hydroxylases and Their Disease-Related Mutant FormsChemical Reviews, 1999
- Structural basis of autoregulation of phenylalanine hydroxylase.Nature Structural & Molecular Biology, 1999
- Structure of Tetrameric Human Phenylalanine Hydroxylase and Its Implications for PhenylketonuriaPublished by Elsevier ,1998
- Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuriaNature Structural & Molecular Biology, 1997
- Structure/Function Relationships in Human Phenylalanine HydroxylaseEuropean Journal of Biochemistry, 1996
- Pterin-Dependent Amino Acid HydroxylasesChemical Reviews, 1996
- Structure and function of the aromatic amino acid hydroxylasesBiochemical Journal, 1995