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Literature summary for 1.14.16.1 extracted from

  • Andersen, O.A.; Stokka, A.J.; Flatmark, T.; Hough, E.
    2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine: substrate specificity and molecular motions related to substrate binding (2003), J. Mol. Biol., 333, 747-757.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
in complex with 6(R)-L-erythro-5,6,7,8-tetrahydrobiopterin and substrate analogues 3-(2-thienyl)-L-alanine or L-norleucine Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00439
-
-

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 substrate binding triggers structural changes throughout the entire tetrameric enzyme Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-(2-thienyl)-L-alanine + tetrahydrobiopterin + O2
-
Homo sapiens ? + dihydrobiopterin + H2O
-
?
L-norleucine + tetrahydrobiopterin + O2 5% of the activity with 3-(2-thienyl)-L-alanine Homo sapiens ? + dihydrobiopterin + H2O
-
?