Regulation of rat liver phenylalanine hydroxylase. II. Substrate binding and the role of activation in the control of enzymatic activity.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference34 articles.
1. Stoichiometric reduction of phenylalanine hydroxylase by its cofactor: a requirement for enzymatic activity
2. Regulation of rat liver phenylalanine hydroxylase. I. Kinetic properties of the enzyme's iron and enzyme reduction site.
3. A simple purification of phenylalanine hydroxylase by substrate-induced hydrophobic chromatography.
4. Substrate activation of phenylalanine hydroxylase. A kinetic characterization.
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1. The aromatic amino acid hydroxylases: Structures, catalysis, and regulation of phenylalanine hydroxylase, tyrosine hydroxylase, and tryptophan hydroxylase;Archives of Biochemistry and Biophysics;2023-02
2. A noncoding RNA modulator potentiates phenylalanine metabolism in mice;Science;2021-08-06
3. Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase;Journal of Biological Chemistry;2016-04
4. The Amino Acid Specificity for Activation of Phenylalanine Hydroxylase Matches the Specificity for Stabilization of Regulatory Domain Dimers;Biochemistry;2015-08-13
5. Activation of Phenylalanine Hydroxylase by Phenylalanine Does Not Require Binding in the Active Site;Biochemistry;2014-12-02
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