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Literature summary for 1.14.16.1 extracted from

  • Patel, D.; Kopec, J.; Fitzpatrick, F.; McCorvie, T.J.; Yue, W.W.
    Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain (2016), Sci. Rep., 6, 23748 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
L-phenylalanine
-
Homo sapiens

Protein Variants

Protein Variants Comment Organism
E76A the mutation is associated with phenylketonuria Homo sapiens
G46S the mutation is associated with phenylketonuria Homo sapiens
I65S the mutation is associated with phenylketonuria Homo sapiens
T63P the mutation is associated with phenylketonuria Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26300
-
catalytic domain, calculated from amino acid sequence Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2 Homo sapiens
-
L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P00439
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2
-
Homo sapiens L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 13500, catalytic domain, calculated from amino acid sequence Homo sapiens

Synonyms

Synonyms Comment Organism
PAH
-
Homo sapiens
phenylalanine hydroxylase
-
Homo sapiens