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Literature summary for 1.14.16.2 extracted from

  • Briggs, G.D.; Bulley, J.; Dickson, P.W.
    Catalytic domain surface residues mediating catecholamine inhibition in tyrosine hydroxylase (2014), J. Biochem., 155, 183-193.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
A297L the Vmax is significantly less reduced by dopamine than for the wild type enzyme Homo sapiens
D361N reductions in Vmax are not significantly different from the wild type enzyme Homo sapiens
E362G the Vmax is reduced compared to the wild type enzyme Homo sapiens
E362Q reductions in Vmax are not significantly different from the wild type enzyme Homo sapiens
E362R/E365R the Vmax is significantly less reduced by dopamine than for the wild type enzyme Homo sapiens
E365G the Vmax is reduced compared to the wild type enzyme Homo sapiens
E365Q the Vmax is significantly less reduced by dopamine than for the wild type enzyme Homo sapiens
K170E/L480A the mutant is inhibited over the same range of dopamine like the wild type enzyme Homo sapiens
K366L reductions in Vmax are not significantly different from the wild type enzyme Homo sapiens
R37E/R38E the KM for tetrahydrobiopterin measured for the mutant is approximately half that of the wild type enzyme and the Vmax is significantly less reduced by dopamine than for the wild type enzyme Homo sapiens
S368A the Vmax is significantly less reduced by dopamine than for the wild type enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
dopamine
-
Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0081
-
L-tyrosine mutant enzyme R37E/R38E, pH and temperature not specified in the publication Homo sapiens
0.014
-
L-tyrosine mutant enzyme K366L, pH and temperature not specified in the publication Homo sapiens
0.015
-
L-tyrosine mutant enzyme E362R/E365R, pH and temperature not specified in the publication Homo sapiens
0.016
-
L-tyrosine wild type enzyme, pH and temperature not specified in the publication Homo sapiens
0.016
-
L-tyrosine mutant enzyme D361N, pH and temperature not specified in the publication Homo sapiens
0.016
-
L-tyrosine mutant enzyme E362G, pH and temperature not specified in the publication Homo sapiens
0.019
-
L-tyrosine mutant enzyme E365G, pH and temperature not specified in the publication Homo sapiens
0.02
-
L-tyrosine mutant enzyme A297L, pH and temperature not specified in the publication Homo sapiens
0.025
-
L-tyrosine mutant enzyme S368A, pH and temperature not specified in the publication Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
4 * 70000, SDS-PAGE Homo sapiens
300000
-
gel filtration Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-tyrosine + tetrahydrobiopterin + O2 Homo sapiens
-
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens P07101
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tyrosine + tetrahydrobiopterin + O2
-
Homo sapiens 3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
?

Subunits

Subunits Comment Organism
homotetramer 4 * 70000, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
tyrosine hydroxylase
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
tetrahydrobiopterin
-
Homo sapiens

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.000595
-
wild type enzyme, pH and temperature not specified in the publication Homo sapiens dopamine
0.000645
-
mutant enzyme K170E/L480A, pH and temperature not specified in the publication Homo sapiens dopamine

General Information

General Information Comment Organism
metabolism the enzyme performs the rate-limiting step in catecholamine synthesis Homo sapiens