phenylalanine hydroxylase

Over 40 different mutations of the phenylalanine hydroxylase gene have been identified.

Normal people produce an enzyme called phenylalanine hydroxylase in their bodies.

Phenylalanine hydroxylase is closely related to two other enzymes:

A lack of the enzyme phenylalanine hydroxylase used in tyrosine synthesis causes phenylketonuria.

The first enzyme found to use tetrahydrobiopterin is phenylalanine hydroxylase (PAH).

Tetrahydrobiopterin works with an enzyme called phenylalanine hydroxylase to process a substance called phenylalanine.

Research on phenylalanine hydroxylase by Seymour Kaufman led to the discovery of tetrahydrobiopterin as a biological cofactor.

The conversion of phe to tyr is catalyzed by the enzyme phenylalanine hydroxylase, a monooxygenase.

Tyrosine is created from phenylalanine by hydroxylation by the enzyme phenylalanine hydroxylase.

Classical PKU refers to persons with 2 severe mutations of the phenylalanine hydroxylase gene.

The aromatic side chain of phenylalanine is hydroxylated by the enzyme phenylalanine hydroxylase to form tyrosine.

Phenylketonuria - A autosomal recessive genetic disorder characterized by a deficiency in the enzyme phenylalanine hydroxylase.

When tetrahydrobiopterin interacts with phenylalanine hydroxylase, tetrahydrobiopterin is altered and must be recycled to a usable form.

Phenylalanine hydroxylase is the rate-limiting enzyme of the metabolic pathway that degrades excess phenylalanine.

Since phenylketonurea can cause irreversible damage, it is imperative that deficiencies in the Phenylalanine Hydroxylase are determined early on in development.

The gene for phenylalanine hydroxylase, which is on chromosome 12, contains 13 exons and messenger RNA is not readily available.

By using virus vectors phenylalanine hydroxylase genes carrying eight different mutations have each been inserted into a hepatoma cell line without natural hydroxylase activity.

Recent work at the University of Leeds has found the parasite produces an enzyme with tyrosine hydroxylase and phenylalanine hydroxylase activity.

Phenylketonuria (PKU) is a metabolic disorder in which the individual is missing an enzyme called phenylalanine hydroxylase.

Using virus vectors, Woo successfully inserted normal mouse genes for phenylalanine hydroxylase into cultured liver cells from the mutant mouse.

However, when the phenylalanine hydroxylase enzyme is absent or deficient, phenylalanine abnormally accumulates in the blood and is toxic to brain tissue.

Except for 1-2% of subjects with defective metabolism of tetrahydrobiopterin, these infants have a recessively inherited deficiency in the hepatic enzyme phenylalanine hydroxylase.

A low phenylalanine diet cannot fully substitute for the fine tuning of phenylalanine turnover normally exerted by hepatic phenylalanine hydroxylase.

For example, the normal sequence of phenylalanine hydroxylase in macaques and chimpanzees is the mutated sequence responsible for phenylketonuria in humans.

The enzyme phenylalanine hydroxylase normally converts the amino acid phenylalanine into the amino acid tyrosine.