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Literature summary for 1.14.16.4 extracted from

  • Pavon, J.A.; Eser, B.; Huynh, M.T.; Fitzpatrick, P.F.
    Single turnover kinetics of tryptophan hydroxylase: evidence for a new intermediate in the reaction of the aromatic amino acid hydroxylases (2010), Biochemistry, 49, 7563-7571.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
truncated version expressed in Escherichia coli Oryctolagus cuniculus

Protein Variants

Protein Variants Comment Organism
DELTA 1-101/DELTA last 28 residues catalytic core Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tryptophan + tetrahydrobiopterin + O2
-
Oryctolagus cuniculus 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin
-
?

Synonyms

Synonyms Comment Organism
tryptophan hydroxylase
-
Oryctolagus cuniculus