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Literature summary extracted from

  • Daubner, S.C.; Avila, A.; Bailey, J.O.; Barrera, D.; Bermudez, J.Y.; Giles, D.H.; Khan, C.A.; Shaheen, N.; Thompson, J.W.; Vasquez, J.; Oxley, S.P.; Fitzpatrick, P.F.
    Mutagenesis of a specificity-determining residue in tyrosine hydroxylase establishes that the enzyme is a robust phenylalanine hydroxylase but a fragile tyrosine hydroxylase (2013), Biochemistry, 52, 1446-1455.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.16.2 expressed in Escherichia coli BL21(DE3) pLysS cells Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.14.16.1 V379D/H264Q the mutant shows significant activity at tyrosine hydroxylation and a 3000fold decrease in preference for phenylalanine over tyrosine as the substrate Homo sapiens
1.14.16.2 D425A the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425C the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425E the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425F the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425G the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425H the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425I the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425K the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425L the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425M the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425N the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425Q the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425R the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425S the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425T the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425V the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 D425W inactive Rattus norvegicus
1.14.16.2 D425Y the mutant shows strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 Q424A the mutant shows reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 Q426A the mutant strongly reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 T427A the mutant shows reduced activity compared to the wild type enzyme Rattus norvegicus
1.14.16.2 Y423A the mutant shows reduced activity compared to the wild type enzyme Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.16.2 0.00105
-
 L-tyrosine mutant enzyme D425T, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0016
-
 L-phenylalanine mutant enzyme D425T, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0053
-
 L-phenylalanine mutant enzyme D425G, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.006
-
 L-tyrosine mutant enzyme D425L, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0069
-
 L-tyrosine mutant enzyme D425M, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0089
-
 L-tyrosine mutant enzyme D425S, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0092
-
 L-phenylalanine mutant enzyme D425S, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0105
-
 L-phenylalanine mutant enzyme D425Y, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0106
-
 L-tyrosine mutant enzyme D425G, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0144
-
 L-phenylalanine mutant enzyme D425F, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0148
-
 L-phenylalanine mutant enzyme D425V, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.015
-
 L-tyrosine mutant enzyme D425C, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0152
-
 L-phenylalanine mutant enzyme D425C, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0164
-
 L-phenylalanine mutant enzyme D425M, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0172
-
 L-tyrosine mutant enzyme D425F, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0187
-
 L-tyrosine mutant enzyme D425H, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.019
-
 L-phenylalanine mutant enzyme D425L, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.021
-
 L-phenylalanine mutant enzyme D425A, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.022
-
 L-phenylalanine mutant enzyme D425I, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.028
-
 L-phenylalanine mutant enzyme D425R, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.03
-
 L-tyrosine mutant enzyme Y423A, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0308
-
 L-tyrosine mutant enzyme D425Y, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.04
-
 L-tyrosine mutant enzyme D425V, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.04
-
 L-tyrosine wild type enzyme, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.041
-
 L-tyrosine mutant enzyme D425I, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.044
-
 L-tyrosine mutant enzyme Q424A, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.045
-
 L-phenylalanine mutant enzyme D425E, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.051
-
 L-tyrosine mutant enzyme T427A, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.056
-
 L-tyrosine mutant enzyme D425A, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.0565
-
 L-phenylalanine mutant enzyme D425Q, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.062
-
 L-phenylalanine mutant enzyme D425N, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.066
-
 L-tyrosine mutant enzyme Q426A, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.088
-
 L-tyrosine mutant enzyme D425R, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.097
-
 L-tyrosine mutant enzyme D425E, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.1
-
 L-phenylalanine wild type enzyme, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.162
-
 L-tyrosine mutant enzyme D425Q, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.172
-
 L-tyrosine mutant enzyme D425N, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 0.2
-
 L-phenylalanine mutant enzyme D425K, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 2.39
-
 L-tyrosine mutant enzyme D425K, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus
1.14.16.2 5
-
 L-phenylalanine mutant enzyme D425H, in 50 mM HEPES (pH 7.0), at 30°C Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.16.1 L-phenylalanine + tetrahydrobiopterin + O2 Homo sapiens
-
 L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?
1.14.16.2 L-tyrosine + tetrahydrobiopterin + O2 Rattus norvegicus best substrate 3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.16.1 Homo sapiens P00439
-
-
1.14.16.2 Rattus norvegicus P04177
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.16.1 L-phenylalanine + tetrahydrobiopterin + O2
-
 Homo sapiens L-tyrosine + 4a-hydroxytetrahydrobiopterin
-
 ?
1.14.16.1 additional information the enzyme is nearly incapable of hydroxylating tyrosine Homo sapiens ?
-
 ?
1.14.16.2 L-phenylalanine + 6-methyltetrahydrobiopterin + O2
-
 Rattus norvegicus ?
-
 ?
1.14.16.2 L-tryptophan + 6-methyltetrahydrobiopterin + O2 worst substrate Rattus norvegicus ?
-
 ?
1.14.16.2 L-tyrosine + 6-methyltetrahydrobiopterin + O2 best substrate Rattus norvegicus 3,4-dihydroxy-L-phenylalanine + 6-methyl-4a-hydroxytetrahydrobiopterin
-
 ?
1.14.16.2 L-tyrosine + tetrahydrobiopterin + O2 best substrate Rattus norvegicus 3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.16.1 PheH
-
 Homo sapiens
1.14.16.1 phenylalanine hydroxylase
-
 Homo sapiens
1.14.16.2 TyrH
-
 Rattus norvegicus
1.14.16.2 tyrosine hydroxylase
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.16.2 tetrahydrobiopterin
-
 Rattus norvegicus