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Literature summary for 1.14.16.1 extracted from

  • Li, J.; Ilangovan, U.; Daubner, S.C.; Hinck, A.P.; Fitzpatrick, P.F.
    Direct evidence for a phenylalanine site in the regulatory domain of phenylalanine hydroxylase (2011), Arch. Biochem. Biophys., 505, 250-255.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
regulatory domain (amino acids 1-118) of rat phenylalanine hydroxylase is expressed in Escherichia coli Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
13000
-
2 * 13000 (regulatory domain 1-118), gel filtration. In the presence of phenylalanine, the protein elutes earlier from the column, consistent with a conformational change in the presence of the amino acid Rattus norvegicus
26000
-
gel filtration, regulatory domain (amino acids 1-118) Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-phenylalanine + a 5,6,7,8-tetrahydropteridine + O2 = L-tyrosine + a 4a-hydroxy-5,6,7,8-tetrahydropteridine 1H-15N HSQC NMR spectra are obtained of the 15N-labeled protein alone and in the presence of phenylalanine. Regulatory domain of phenylalanine hydroxylase can bind phenylalanine, consistent with the presence of an allosteric site for the amino acid Rattus norvegicus

Subunits

Subunits Comment Organism
dimer 2 * 13000 (regulatory domain 1-118), gel filtration. In the presence of phenylalanine, the protein elutes earlier from the column, consistent with a conformational change in the presence of the amino acid Rattus norvegicus

Synonyms

Synonyms Comment Organism
phenylalanine hydroxylase
-
Rattus norvegicus