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Literature summary for 1.14.16.1 extracted from

  • Daubner, S.C.; Hillas, P.J.; Fitzpatrick, P.F.
    Expression and characterization of the catalytic domain of human phenylalanine hydroxylase (1997), Arch. Biochem. Biophys., 348, 295-302.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
truncated enzyme containing the C-terminal 336 amino acids bearing the catalytic domain Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.024
-
tryptophan truncated enzyme containing C-terminal 334 amino acids, pH 8.0 Homo sapiens
0.041
-
tetrahydrobiopterin truncated enzyme containing C-terminal 334 amino acids Homo sapiens
0.053
-
tetrahydrobiopterin recombinant enzyme Homo sapiens
0.085
-
6-methyltetrahydropterin truncated enzyme containing C-terminal 334 amino acids Homo sapiens
0.096
-
tryptophan truncated enzyme containing C-terminal 334 amino acids, pH 7.0 Homo sapiens
0.1
-
6-methyltetrahydropterin recombinant enzyme Homo sapiens
0.145
-
L-phenylalanine truncated enzyme containing C-terminal 334 amino acids Homo sapiens
0.329
-
L-phenylalanine recombinant enzyme Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
truncated enzyme containing the C-terminal 343 amino acids Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
14
-
truncated enzyme containing C-terminal 334 amino acids Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + tetrahydrobiopterin + O2 truncated enzyme containing C-terminal 334 amino acids Homo sapiens ?
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.53
-
phenylalanine truncated enzyme containing C-terminal 334 amino acids Homo sapiens
6.58
-
phenylalanine recombinant wild-type enzyme Homo sapiens