Phenylalanine hydroxylase

PAH
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1DMW, 1J8T, 1J8U, 1KW0, 1LRM, 1MMK, 1MMT, 1TDW, 1TG2, 2PAH, 3PAH, 4ANP, 5PAH, 6PAH, 5FII
Identifiers
Aliases	PAH, PH, PKU, PKU1, phenylalanine hydroxylase
External IDs	OMIM: 612349; MGI: 97473; HomoloGene: 234; GeneCards: PAH; OMA:PAH - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	102,958,410 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	87,419,998 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; gallbladder; ; kidney tubule; ; glomerulus; ; metanephric glomerulus; ; body of pancreas; ; renal medulla; ; human kidney; ; testicle; ; sperm;
	Top expressed in
	left lobe of liver; ; human kidney; ; right kidney; ; gallbladder; ; proximal tubule; ; pyloric antrum; ; human fetus; ; fetal liver hematopoietic progenitor cell; ; pancreas; ; sexually immature organism;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	iron ion binding; phenylalanine 4-monooxygenase activity; metal ion binding; monooxygenase activity; catalytic activity; 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
	5053
	18478
	ENSG00000171759
	ENSMUSG00000020051
	P00439
	P16331
	NM_000277; NM_001354304
	NM_008777
	NP_000268; NP_001341233
	NP_032803
	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.

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000171759 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: 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.
^ Fitzpatrick PF (1999). "Tetrahydropterin-dependent amino acid hydroxylases". Annual Review of Biochemistry. 68: 355–81. doi:10.1146/annurev.biochem.68.1.355. PMID 10872454.
^ 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.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000171759 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020051 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[Fitzpatrick1999-5] Fitzpatrick PF (1999). "Tetrahydropterin-dependent amino acid hydroxylases". Annual Review of Biochemistry. 68: 355–81. doi:10.1146/annurev.biochem.68.1.355. PMID 10872454.

[pmid13525410-6] 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.

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