Structure of phenylalanine hydroxylase from Colwellia psychrerythraea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stability. J. Biol. Chem. 2007; 282:21973-21986. [PubMed: 17537732]
APHENYLALANINE HYDROXYLASE MammalianPAHis a cytoplasmicenzymemainly located in the liver and in the kidneys. A dysfunctional PAH, usually due to mutations in the gene coding for the enzyme, is associated with the disorder Følling’s disease orphenylketonuria(PKU; [Mendelian Inheritance in Man number...
Phenylalanine hydroxylase (PAH; EC 1.14.16.1) is an important metabolic enzyme, belonging to the aromatic amino acid hydroxylase (AAAH) family1, that catalyzes the conversion of phenylalanine (Phe) to tyrosine (Tyr) in a tetrahydrobiopterin (BH4)-dependent reaction2. This mixed-function monooxygenas...
Mutational spectrum of phenylalanine hydroxylase deficiency in Sicily: implications for diagnosis of hyperphenylalaninemia in southe... Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria ...
the carbodiimide-promoted coupling of a carboxyl group to N-5 of a tetrahydropterin, is described.3Two novel adsorbents, 5-formyl-tetrahydrofolate–AH-Sepharose and 5-methyl-tetrahydrofolate–AH-Sepharose, are described which may be useful not only in the study of phenylalanine hydroxylase but als...
Phenylketonuria (PKU, OMIM 261600) is an autosomal recessive disorder caused by a deficiency of phenylalanine hydroxylase (PAH). Reduced PAH activity causes high phenylalanine concentrations in blood and tissues, and if untreated, results in microcephaly, severe developmental delay, epilepsy, and irrevers...
It appears in large amount in urine of patients with phenylketonuria which is a human genetic disorder due to the lack of phenylalanine hydroxylase, the enzyme necessary to metabolize phenylalanine to tyrosine. Acetylphenylalanine is a product of enzyme phenylalanine N-acetyltransferase in the pathway ...
Phenylalanine hydroxylase (PH; EC 1.14.16.1) is a complex enzyme with three substrates and three activators. Little is known about the structural features which are necessary for the function of this enzyme; only the phosphorylation site is known (Wretburn et al ., 1980). We have recently ...
Its oncogenic action appears due to its ability to inhibit prolyl hydroxylase-containing enzymes. Endogenous Metabolite $32 In Stock Size QTY Naringin Naringoside T059510236-47-2 Naringin (Naringoside), a flavanone glycoside, exerts various of pharmacological effects such as blood lipid lowering, ...
Specific interaction of the diastereomers 7(R)- and 7(S)-tetrahydrobiopterin with phenylalanine hydroxylase: implications for understanding primapterinuria and vitiligo . FASEB J. 20 , 2130 – 2132 .Pey, A. L.; Martinez, A.; Charubala, R.; Maitland, D. J.; Teigen, K.; Calvo, A.; ...