oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
oxidoreductase activity
Cellular component
cytosol
Biological process
catecholamine biosynthetic process
neurotransmitter biosynthetic process
L-phenylalanine catabolic process
cellular amino acid biosynthetic process
aromatic amino acid family metabolic process
metabolism
tyrosine biosynthetic process
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
5053
18478
Ensembl
ENSG00000171759
ENSMUSG00000020051
UniProt
P00439
P16331
RefSeq (mRNA)
NM_000277 NM_001354304
NM_008777
RefSeq (protein)
NP_000268 NP_001341233
NP_032803
Location (UCSC)
Chr 12: 102.84 – 102.96 Mb
Chr 10: 87.36 – 87.42 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Phenylalanine hydroxylase (PAH) (EC 1.14.16.1) is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine. PAH is one of three members of the biopterin-dependent aromatic amino acid hydroxylases, a class of monooxygenase that uses tetrahydrobiopterin (BH4, a pteridine cofactor) and a non-heme iron for catalysis. During the reaction, molecular oxygen is heterolytically cleaved with sequential incorporation of one oxygen atom into BH4 and phenylalanine substrate.[5][6] In humans, mutations in its encoding gene, PAH, can lead to the metabolic disorder phenylketonuria.
Reaction catalyzed by PAH
^ abcGRCh38: Ensembl release 89: ENSG00000171759 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000020051 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Kaufman S (February 1958). "A new cofactor required for the enzymatic conversion of phenylalanine to tyrosine". The Journal of Biological Chemistry. 230 (2): 931–9. doi:10.1016/S0021-9258(18)70516-4. PMID 13525410.
and 25 Related for: Phenylalanine hydroxylase information
Phenylalaninehydroxylase (PAH) (EC 1.14.16.1) is an enzyme that catalyzes the hydroxylation of the aromatic side-chain of phenylalanine to generate tyrosine...
nonfunctional phenylalaninehydroxylase, an enzyme responsible for the metabolism of excess phenylalanine. This results in the buildup of dietary phenylalanine to...
Tyrosine hydroxylase, phenylalaninehydroxylase and tryptophan hydroxylase together make up the family of aromatic amino acid hydroxylases (AAAHs). Tyrosine...
fight-or-flight response. Tyrosine is created from phenylalanine by hydroxylation by the enzyme phenylalaninehydroxylase. Tyrosine is also ingested directly from...
phenylketonuria (PKU) is the inability to metabolize phenylalanine because of a lack of the enzyme phenylalaninehydroxylase. Individuals with this disorder are known...
hydroxylase, phenylalaninehydroxylase, and tryptophan hydroxylase together constitute the family of biopterin-dependent aromatic amino acid hydroxylases. TPH...
cofactor of the three aromatic amino acid hydroxylase enzymes, used in the degradation of amino acid phenylalanine and in the biosynthesis of the neurotransmitters...
17α-Hydroxylase Cholesterol 7 alpha-hydroxylase Dopamine β-hydroxylasePhenylalaninehydroxylase Tyrosine hydroxylase One example of non-biological hydroxylation is...
defect in a single gene on chromosome 12 that codes for enzyme phenylalaninehydroxylase, that affects multiple systems, such as the nervous and integumentary...
failure to convert phenylalanine to tyrosine as a result of the entire or partial absence of the enzyme phenylalaninehydroxylase. The coloration of the...
acid, by phenylalaninehydroxylase. However, this enzyme requires tetrahydrobiopterin as a cofactor and thus its deficiency slows phenylalanine metabolism...
inability to breakdown phenylalanine, is due to a lack of the enzyme phenylalaninehydroxylase. A dietary lack of tryptophan can cause stunted skeletal development...
the enzyme phenylalaninehydroxylase, which catalyzes the first step in the degradation of phenylalanine, result in build-up of phenylalanine and related...
perform its neuronal activity. L-Phenylalanine is converted into L-tyrosine by the enzyme phenylalaninehydroxylase, with molecular oxygen (O2) and tetrahydrobiopterin...
Tetrahydrobiopterin works with an enzyme called phenylalaninehydroxylase to process a substance called phenylalanine. Phenylalanine is an amino acid (a building block...
with tyrosine being the most common. Phenylalanine is converted into tyrosine by the enzyme phenylalaninehydroxylase, with molecular oxygen (O2) and tetrahydrobiopterin...
amino acid phenylalanine (Phe), which is derived from food. The conversion of Phe to Tyr is catalyzed by the enzyme phenylalaninehydroxylase, a monooxygenase...
oxidative deamination of phenylalanine. When the activity of the enzyme phenylalaninehydroxylase is reduced, the amino acid phenylalanine accumulates and gets...
of benzylisoquinoline. First, the amino acid phenylalanine, through the enzyme phenylalaninehydroxylase, is transformed into tyrosine. Tyrosine can follow...
punishment from its unpleasant effects deters drug consumption. Phenylalaninehydroxylase inhibitors like 3,4-dihydroxystyrene), which is currently only...
central nervous system: 5-HTP to serotonin Tryptophan to tryptamine Phenylalanine to phenethylamine L-tyrosine to tyramine Centrally mediated side effects...
Global Information
