Results 251 to 260 of about 152,932 (290)
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Hepatic Phenylalanine Hydroxylase and PKU
1975The conversion of phenylalanine to tyrosine in mammalian tissues is catalyzed by a complex enzyme system composed of several essential enzymes and cofactors. All of these components have been assayed in liver biopsy samples from patients with the classic form of PKU.
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Phenylalanine Hydroxylase Activity-Reply
Archives of Pediatrics & Adolescent Medicine, 1983In Reply .—For most metabolic disorders, a diagnosis based on a single symptom would not be acceptable. Hyperphenylalaninemia is a symptom that in a newborn infant suggests either complete or partial PH deficiency (PKU), dihydropteridine reductase deficiency, or deficiency in biopterin synthesis.
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Regulation of the activity of hepatic phenylalanine hydroxylase
Advances in Enzyme Regulation, 1986Rat liver phenylalanine hydroxylase catalyzes the tetrahydropterin-dependent oxidation of phenylalanine to tyrosine, according to equation 1. In addition to the naturally-occurring coenzyme, tetrahydrobiopterin (BH4), certain synthetic analogs of BH4 such as 6-methyltetrahydropterin (6MPH4) have high cofactor activity.
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Thermal profiling reveals phenylalanine hydroxylase as an off-target of panobinostat.
Nature Chemical Biology, 2016Isabelle Becher +12 more
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On the mechanism of action of phenylalanine hydroxylase
Biochemical Society Transactions, 1985Thomas A. Dix +6 more
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Effects of phenylalanine on phenylalanine hydroxylase separation and stability
Biochemical Medicine, 1985Ennis C. Layne +2 more
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Tetrahydrobipterin-responsive phenylalanine hydroxylase deficiency
Journal of Human Genetics, 2018S. Kure, H. Shintaku
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[74] Phenylalanine hydroxylase (Pseudomonas)
1970Publisher Summary This chapter discusses the assay, purification, and properties of phenylalanine hydroxylase from Pseudomonas. The hydroxylation of phenylalanine to tyrosine is catalyzed by an inducible enzyme from Pseudomonas. This conversion requires molecular oxygen and a tetrahydropteridine.
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