What does the enzyme phenylalanine hydroxylase do?
Phenylalanine hydroxylase is responsible for the conversion of phenylalanine to another amino acid, tyrosine. The enzyme works with a molecule called tetrahydrobiopterin (BH4) to carry out this chemical reaction.
What is human phenylalanine hydroxylase gene?
Summary. This gene encodes a member of the biopterin-dependent aromatic amino acid hydroxylase protein family. The encoded phenylalanine hydroxylase enzyme hydroxylates phenylalanine to tyrosine and is the rate-limiting step in phenylalanine catabolism.
Where is the phenylalanine hydroxylase gene?
Phenylalanine hydroxylase
| PAH | |
|---|---|
| External IDs | OMIM: 612349 MGI: 97473 HomoloGene: 234 GeneCards: PAH |
| showGene location (Human) | |
| showGene location (Mouse) | |
| showRNA expression pattern |
What happens when phenylalanine accumulates in the body?
Phenylalanine is an essential nutrient, but some individuals are born with a genetic disorder, phenylketonuria (PKU), that prevents them from metabolizing phenylalanine, and, if untreated, phenylalanine accumulates in the body, becomes converted into phenylpyruvate, and the individual usually develops seizures, brain …
What is the expected result of a deficiency in the enzyme phenylalanine hydroxylase?
As Phe is an essential amino acid, having inadequate phenylalanine leads to growth restriction, microcephaly, and developmental problems. The safety of dietary restriction of Phe for individuals with the milder PAH deficiency has not been systematically studied.
Can a parent who does not have PKU have a child with PKU?
PKU is passed on to children when each parent has 1 mutated gene. This means that neither parent has any symptoms of PKU, but both are carriers of the faulty gene. PKU is an autosomal recessive disease. This means that a child needs to inherit 1 faulty gene from each parent to show signs of the disorder.
Where is phenylalanine hydroxylase found in the cell?
Liver cells
Liver cells contain an enzyme called phenylalanine hydroxylase, which can add this group and convert phenylalanine to tyrosine. Thus as long as this enzyme is functional and there is a reasonable supply of phenylalanine, tyrosine can be synthesized in your body and does not have to be included in the food that you eat.
What are the symptoms of phenylalanine deficiency?
Symptoms
- A musty odor in the breath, skin or urine, caused by too much phenylalanine in the body.
- Neurological problems that may include seizures.
- Skin rashes (eczema)
- Fair skin and blue eyes, because phenylalanine can’t transform into melanin — the pigment responsible for hair and skin tone.
What is phenylalanine hydroxylase?
Phenylalanine is found in all proteins and in some artificial sweeteners. Phenylalanine hydroxylase is responsible for the conversion of phenylalanine to another amino acid, tyrosine.
What is the Pah hydroxylase gene?
PAH phenylalanine hydroxylase [ (human)] Summary. This gene encodes a member of the biopterin-dependent aromatic amino acid hydroxylase protein family. The encoded phenylalanine hydroxylase enzyme hydroxylates phenylalanine to tyrosine and is the rate-limiting step in phenylalanine catabolism.
What is the pah-exon1 deleted murine model of phenylalanine hydroxylase deficiency?
A novel Pah-exon1 deleted murine model of phenylalanine hydroxylase (PAH) deficiency. Molecular characterization of Thai patients with phenylalanine hydroxylase deficiency and in vitro functional study of two novel PAH variants. A porcine model of phenylketonuria generated by CRISPR/Cas9 genome editing.
What are the hot spots of phenylalanine hydroxylase (PAH) mutation?
We sequenced the entire gene for phenylalanine hydroxylase in 51 unrelated hyperphenylalaninemia patients from Southern Italy Study demonstrated the variety of the mutation type PAH gene of PKU in Inner Mongolia population, and confirmed that R243Q, Y356X, Y204C were the hot spots of PAH gene mutation.