Phenylalanine hydroxylase

PAH
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPAH, PH, PKU, PKU1, phenylalanine hydroxylase
External IDsOMIM: 612349 MGI: 97473 HomoloGene: 234 GeneCards: PAH
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000277
NM_001354304

NM_008777

RefSeq (protein)

NP_000268
NP_001341233

NP_032803

Location (UCSC)Chr 12: 102.84 – 102.96 MbChr 10: 87.36 – 87.42 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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.
Reaction catalyzed by PAH
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000171759 - Ensembl, May 2017
  2. ^ a b c 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.
  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.
  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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