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Oxidoreductases | Transferases | Hydrolases | Lyases | Isomerases | Ligases |
Basic Information |
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Enzyme Number | 1.14.16.1 |
Official Name | phenylalanine 4-monooxygenase |
Name from literature | phenylalanine hydroxylase |
Pathway from literature | hepatic phenylalanine metabolism |
Pathway from KEGG |
Amino Acid Metabolism; Phenylalanine, tyrosine and tryptophan biosynthesis; map00400 |
Organisms | Mouse (10090) |
Genome localization | 10 C2-D1|10 47.0 cM[18478 ], |
Comments | The active centre contains mononuclear iron(II). The reaction involves an arene oxide that rearranges to give the phenolic hydroxy group. This results in the hydrogen at C-4 migrating to C-3 and in part being retained. This process is known as the NIH-shift. The 4a-hydroxytetrahydrobiopterin formed can dehydrate to 6,7-dihydrobiopterin, both spontaneously and by the action of EC 4.2.1.96, 4a-hydroxytetrahydrobiopterin dehydratase. The 6,7-dihydrobiopterin can be enzymically reduced back to tetrahydrobiopterin, by EC 1.5.1.34, 6,7-dihydropteridine reductase, or slowly rearranges into the more stable compound 7,8-dihydrobiopterin. |
Rate-limiting Description | "The guanosine triphosphate (GTP) cyclohydrolase I (GTP-CHI) catalyses the rate-limiting step in the de novo synthesis of tetrahydrobiopterin, a cofactor of three aromatic amino acid hydroxylases, one of which is phenylalanine hydroxylase." (10984661) |
Regulatory Information |
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Regulatory type | Detail |
phosphorylation; | P16331 |
phosphorylation; | P16331:from_uniprot:16_Phosphoserine; by PKA |
Gene ontology |
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Gene ontology |
GO:0016597 (F) amino acid binding [P16331 ]; |
Disease relevance |
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Disease |
Mouse strains deficient in phenylalanine hydroxylase (Pah) were created as models of phenylketonuria (PKU) [P16331 ]; |
Links |
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SwissProt | |
Entrez Gene |
Copyright 2009, Center for Bioinformatics | |||
Last Modified: 2009-03-24 | |||
Design by Zhao Min |