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Literature summary for 1.14.16.4 extracted from

  • McKinney, J.; Teigen, K.; Froystein, N.A.; Salauen, C.; Knappskog, P.M.; Haavik, J.; Martinez, A.
    Conformation of the substrate and pterin cofactor bound to human tryptophan hydroxylase. Important role of Phe313 in substrate specificity (2001), Biochemistry, 40, 15591-15601.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression of full-length and N-terminal truncated enzyme in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
F313W N-terminal truncated enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
L-erythro-7,8-dihydrobiopterin recombinant N-terminal truncated enzyme, competitive vs. (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.017
-
 L-tryptophan F313W mutant, recombinant N-terminal truncated enzyme Homo sapiens
0.022
-
 L-phenylalanine F313W mutant, recombinant N-terminal truncated enzyme Homo sapiens
0.033
-
 L-tryptophan recombinant N-terminal truncated enzyme Homo sapiens
0.048
-
 L-phenylalanine recombinant N-terminal truncated enzyme Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ Fe2+ concentration for half-maximal activation of recombinant N-terminal truncated enzyme: 0.0013 mM Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant full-length and N-terminal truncated enzyme Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2
-
 Homo sapiens L-tyrosine + dihydropterin + H2O
-
 r

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.161
-
 L-erythro-7,8-dihydrobiopterin recombinant truncated enzyme Homo sapiens