Identification of the Allosteric Site for Phenylalanine in Rat Phenylalanine Hydroxylase
نویسندگان
چکیده
منابع مشابه
Mechanism of phenylalanine regulation of phenylalanine hydroxylase.
The mechanism of phenylalanine regulation of rat liver phenylalanine hydroxylase was studied. We show that phenylalanine "activates" phenylalanine hydroxylase, converting it from an inactive to active form, by binding at a true allosteric regulatory site. One phenylalanine molecule binds per enzyme subunit; it remains at this site during catalytic turnover and, while there, cannot be hydroxylat...
متن کاملRegulation of Rat Liver Phenylalanine Hydroxylase
Effects of phenylalanine and diand tetrahydropterins on presteady-state and steady-state catalytic behavior of rat liver phenylalanine hydroxylase are analyzed. From this and previous work (Shiman, R, Xia, T., Hill, M., and Gray, D. (1994) J. BioZ. Chem. 269, 2464724656), which analyzed binding of the same compounds to the enzyme in the absence of catalysis, a model of phenylalanine hydroxylase...
متن کاملImmunocytochemical Identification of Phenylalanine Hydroxylase and Albumin
Rhodamine-conjugated antibodies specific for phenylalanine hydroxylase and serum albumin were employed as cytochemical probes to identify these two proteins in H4 hepatoma cells and in isolated rat hepatocytes . Each fluorescent antibody stained the cells specifically and in a distinctive manner . In both cell types, albumin staining was discretely localized in cytoplasmic "bundles," whereas, p...
متن کاملActivation of Phenylalanine Hydroxylase by Phenylalanine Does Not Require Binding in the Active Site
Phenylalanine hydroxylase (PheH), a liver enzyme that catalyzes the hydroxylation of excess phenylalanine in the diet to tyrosine, is activated by phenylalanine. The lack of activity at low levels of phenylalanine has been attributed to the N-terminus of the protein's regulatory domain acting as an inhibitory peptide by blocking substrate access to the active site. The location of the site at w...
متن کاملMouse phenylalanine hydroxylase. Homology and divergence from human phenylalanine hydroxylase.
The laboratory mouse represents an important model for the study of phenylalanine metabolism and the pathochemistry of phenylketonuria, yet mouse phenylalanine hydroxylase (PAH) has not been extensively studied. We report the cloning and sequencing of a mouse PAH cDNA, the expression of enzymic activity from the mouse PAH cDNA clone and the identification of mouse PAH and human PAH by two-dimen...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2016
ISSN: 0021-9258
DOI: 10.1074/jbc.m115.709998