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Literature summary for 1.14.16.2 extracted from

  • Goodwill, K.E.; Sabatier, C.; Stevens, R.C.
    Crystal structure of tyrosine hydroxylase with bound cofactor analog and iron at 2.3.ANG. resolution: self-hydroxylation of Phe300 and the pterin-binding site (1998), Biochemistry, 37, 13437-13445.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
3D-structure model, ligand binding of pterin analogues Rattus norvegicus
crystals of the binary complex with iron and 7,8-dihydrobiopterin obtained by equilibrium dialysis, solutions degassed by helium and crystal growth in nitrogen atmosphere at 4°C Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information investigation of the role of several amino acid residues in binding of substrate and ligands by site-specific mutagenesis Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
5-[(3-azido-6-nitrobenzylidene)amino]-2,6-diamino-4-pyrimidinone competitive against tetrahydrobiopterin Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant from Escherichia coli Rattus norvegicus

Reaction

Reaction Comment Organism Reaction ID
L-tyrosine + a 5,6,7,8-tetrahydropteridine + O2 = L-dopa + a 4a-hydroxy-5,6,7,8-tetrahydropteridine stereochemical analysis of ligand binding Rattus norvegicus
a
L-tyrosine + a 5,6,7,8-tetrahydropteridine + O2 = L-dopa + a 4a-hydroxy-5,6,7,8-tetrahydropteridine active binding site Rattus norvegicus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tyrosine + 6-methyltetrahydropterin + O2
-
 Rattus norvegicus ?
-
 ?
L-tyrosine + tetrahydrobiopterin + O2
-
 Rattus norvegicus 3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O 3,4-dihydroxy-L-phenylalanine is identical with dopa ?