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
- 14 October 2003
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 333 (4) , 747-757
- https://doi.org/10.1016/j.jmb.2003.09.004
Abstract
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This publication has 35 references indexed in Scilit:
- Substrate-induced conformational transition in human phenylalanine hydroxylase as studied by surface plasmon resonance analyses: the effect of terminal deletions, substrate analogues and phosphorylationBiochemical Journal, 2003
- Crystal Structure of the Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Tetrahydrobiopterin and 3-(2-Thienyl)-l-alanine, and its Implications for the Mechanism of Catalysis and Substrate ActivationJournal of Molecular Biology, 2002
- 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
- The structural basis of the recognition of phenylalanine and pterin cofactors by phenylalanine hydroxylase: implications for the catalytic mechanism 1 1Edited by D. C. ReesJournal of Molecular Biology, 1999
- Structural Insight into the Aromatic Amino Acid Hydroxylases and Their Disease-Related Mutant FormsChemical Reviews, 1999
- Human Phenylalanine Hydroxylase Gene Expression in Kidney and Other Nonhepatic TissuesMolecular Genetics and Metabolism, 1999
- Pterin-Dependent Amino Acid HydroxylasesChemical Reviews, 1996
- Catecholamines in Human Keratinocyte DifferentiationJournal of Investigative Dermatology, 1995
- Characterization of phenylalanine hydroxylase from rat kidneyInternational Journal of Biochemistry, 1993
- The effect of ligands of phenylalanine 4-monooxygenase on the cAMP-dependent phosphorylation of the enzyme.Published by Elsevier ,1984