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Literature summary for 1.14.16.1 extracted from

  • Li, J.; Fitzpatrick, P.F.
    Characterization of metal ligand mutants of phenylalanine hydroxylase: Insights into the plasticity of a 2-histidine-1-carboxylate triad (2008), Arch. Biochem. Biophys., 475, 164-168.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.16.1

Protein Variants

Protein Variants Comment Organism
E330H site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows over 80% reduced activity compared to the wild-type enzyme Rattus norvegicus
E330Q site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows over 80% reduced activity compared to the wild-type enzyme Rattus norvegicus
H285E site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows over 80% reduced activity compared to the wild-type enzyme Rattus norvegicus
H285Q site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows 80% reduced activity compared to the wild-type enzyme Rattus norvegicus
H290E site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows over 80% reduced activity compared to the wild-type enzyme Rattus norvegicus
H290Q site-directed mutagenesis of a metal ligand binding residue, the mutant enzyme shows over 80% reduced activity compared to the wild-type enzyme Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information binding constants for Fe2+ of wild-type and mutant enzymes, overview Rattus norvegicus
0.43
-
 L-Phe pH 7.0, 25°C, wild-type enzyme Rattus norvegicus
0.43
-
 6-methyltetrahydrobiopterin pH 7.0, 25°C, wild-type enzyme Rattus norvegicus
0.43
-
 6-methyltetrahydrobiopterin pH 7.0, 25°C, mutant E330H Rattus norvegicus
0.43
-
 6-methyltetrahydrobiopterin pH 7.0, 25°C, mutant H285E Rattus norvegicus
1.2
-
 L-Phe pH 7.0, 25°C, mutant H290Q Rattus norvegicus
1.2
-
 6-methyltetrahydrobiopterin pH 7.0, 25°C, mutant H290Q Rattus norvegicus
1.6
-
 L-Phe pH 7.0, 25°C, mutant E330Q Rattus norvegicus
1.6
-
 6-methyltetrahydrobiopterin pH 7.0, 25°C, mutant E330Q Rattus norvegicus
3.4
-
 L-Phe pH 7.0, 25°C, mutant H290E Rattus norvegicus
3.4
-
 6-methyltetrahydrobiopterin pH 7.0, 25°C, mutant H290E Rattus norvegicus
6.9
-
 L-Phe pH 7.0, 25°C, mutant H285Q Rattus norvegicus
6.9
-
 6-methyltetrahydrobiopterin pH 7.0, 25°C, mutant H285Q Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ nonheme iron is bound on one face by residues His285, His290, and Glu330 forming a a 2-His-1-carboxylate facial triad, the three ligands differ in their sensitivity to mutagenesis, structure, overview Rattus norvegicus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-phenylalanine + tetrahydrobiopterin + O2 Rattus norvegicus
-
 L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-phenylalanine + 6-methyltetrahydrobiopterin + O2
-
 Rattus norvegicus L-tyrosine + 6-methyl-4a-hydroxytetrahydrobiopterin
-
 ?
L-phenylalanine + tetrahydrobiopterin + O2
-
 Rattus norvegicus L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?

Synonyms

Synonyms Comment Organism
PAH
-
 Rattus norvegicus
phenylalanine hydroxylase
-
 Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Rattus norvegicus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
6-methyltetrahydrobiopterin
-
 Rattus norvegicus
tetrahydrobiopterin
-
 Rattus norvegicus