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3,4-dihydroxy-L-phenylalanine + 6,7-dimethyltetrahydropteridine + O2
?
3,4-dihydroxy-L-phenylalanine + tetrahydropterin + O2
?
4-bromo-L-phenylalanine + 6-methyltetrahydropterin + O2
?
-
low activity
-
-
?
4-chloro-L-phenylalanine + 6-methyltetrahydropterin + O2
?
-
-
-
-
?
4-fluoro-L-phenylalanine + 6-methyltetrahydropterin + O2
?
-
-
-
-
?
4-methoxy-L-phenylalanine + 6-methyltetrahydropteridine + O2
?
-
-
-
-
?
4-methyl-L-phenylalanine + 6-methyltetrahydropterin + O2
?
-
-
-
-
?
L-phenylalanine + 6-methyltetrahydrobiopterin + O2
?
-
-
-
?
L-phenylalanine + tetrahydrobiopterin + O2
L-tyrosine + 3-hydroxyphenylalanine + dihydropteridine + H2O
the enzyme prefers L-tyrosine as a substrate over L-phenylalanine by an order of magnitude
-
-
?
L-phenylalanine + tetrahydropteridine + 2 O2
3,4-dihydroxy-L-phenylalanine + dihydropteridine + 2 H2O
L-phenylalanine + tetrahydropteridine + O2
L-tyrosine + dihydropteridine + H2O
L-tryptophan + 6-methyltetrahydrobiopterin + O2
?
worst substrate
-
-
?
L-tryptophan + tetrahydrobiopterin + O2
?
the enzyme prefers L-tyrosine as a substrate over L-tryptophan by 25fold
-
-
?
L-Tyr + DL-6-methyl-5,6,7,8-tetrahydropterin + O2
?
-
significant activity at a concetration of DL-6-methyl-5,6,7,8-tetrahydropterine: 1.5 mM
-
-
?
L-tyrosine + (6R)-5,6,7,8-tetrahydrobiopterin + O2
3,4-dihydroxyphenylalanine + ?
-
-
-
-
?
L-tyrosine + (6R)-L-erythro-1',2'-dihydroxypropyltetrahydropterin + O2
?
L-tyrosine + (6R)-L-erythro-tetrahydrobiopterin + O2
?
L-tyrosine + (6RS)-L-erythro-tetrahydrobiopterin + O2
?
-
-
-
-
?
L-tyrosine + (6S)-L-erythro-tetrahydrobiopterin + O2
?
-
-
-
-
?
L-tyrosine + 2-amino-4-hydroxy-6,7-dimethyltetrahydropterin + O2
?
L-tyrosine + 2-amino-4-hydroxy-6-methyltetrahydropterin + O2
?
L-tyrosine + 2-methyl-4-oxo-5,6,7,8-tetrahydropterin + O2
?
-
recombinant hTH1
-
-
?
L-tyrosine + 5,6,7,8,-tetrahydro-L-biopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydro-L-biopterin
-
-
-
-
?
L-tyrosine + 5,6,7,8-tetrahydro-L-biopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydro-L-biopterin
L-tyrosine + 5,6,7,8-tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
L-tyrosine + 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine + O2
3,4-dihydroxyphenylalanine + ?
L-tyrosine + 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine + O2
?
L-tyrosine + 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydropteridine + O2
3,4-dihydroxy-L-phenylalanine + ?
-
-
-
-
?
L-tyrosine + 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydropteridine + O2
?
-
-
-
-
?
L-tyrosine + 6-methyl-5,6,7,8-tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 6-methyl-4a-hydroxytetrahydrobiopterin
-
-
-
-
r
L-tyrosine + 6-methyl-tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 6-methyl-4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-tyrosine + 6-methyltetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 6-methyl-4a-hydroxytetrahydrobiopterin
L-tyrosine + 6-methyltetrahydropterin + O2
?
L-tyrosine + ascorbate + O2
3,4-dihydroxy-L-phenylalanine + dehydroascorbate + H2O
-
-
-
?
L-tyrosine + DL-6-methyl-5,6,7,8-tetrahydropterin + O2
?
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
L-tyrosine + tetrahydrofolic acid + O2
?
-
-
-
-
?
L-tyrosine + tetrahydropteridine + O2
3,4-dihydroxyphenylalanine + dihydropteridine + H2O
-
-
-
-
?
L-tyrosine + tetrahydropterin + O2
?
-
-
-
-
?
tyramine + tetrahydrobiopterin + O2
dopamine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
additional information
?
-
3,4-dihydroxy-L-phenylalanine + 6,7-dimethyltetrahydropteridine + O2
?
-
i.e. L-dopa
-
-
?
3,4-dihydroxy-L-phenylalanine + 6,7-dimethyltetrahydropteridine + O2
?
-
L-dopa-oxidase activity
-
-
?
3,4-dihydroxy-L-phenylalanine + tetrahydropterin + O2
?
-
i.e. L-dopa
-
-
?
3,4-dihydroxy-L-phenylalanine + tetrahydropterin + O2
?
-
4 isoforms, thiols required, stimulation by Fe2+ and tetrahydropterin
-
-
?
L-phenylalanine + tetrahydropteridine + 2 O2
3,4-dihydroxy-L-phenylalanine + dihydropteridine + 2 H2O
-
-
-
?
L-phenylalanine + tetrahydropteridine + 2 O2
3,4-dihydroxy-L-phenylalanine + dihydropteridine + 2 H2O
-
-
-
-
?
L-phenylalanine + tetrahydropteridine + 2 O2
3,4-dihydroxy-L-phenylalanine + dihydropteridine + 2 H2O
-
-
-
-
?
L-phenylalanine + tetrahydropteridine + 2 O2
3,4-dihydroxy-L-phenylalanine + dihydropteridine + 2 H2O
-
-
-
?
L-phenylalanine + tetrahydropteridine + 2 O2
3,4-dihydroxy-L-phenylalanine + dihydropteridine + 2 H2O
-
-
-
?
L-phenylalanine + tetrahydropteridine + 2 O2
3,4-dihydroxy-L-phenylalanine + dihydropteridine + 2 H2O
wild-type and mutants
-
?
L-phenylalanine + tetrahydropteridine + O2
L-tyrosine + dihydropteridine + H2O
-
-
-
?
L-phenylalanine + tetrahydropteridine + O2
L-tyrosine + dihydropteridine + H2O
-
-
-
-
?
L-phenylalanine + tetrahydropteridine + O2
L-tyrosine + dihydropteridine + H2O
-
-
-
-
?
L-phenylalanine + tetrahydropteridine + O2
L-tyrosine + dihydropteridine + H2O
-
-
-
?
L-phenylalanine + tetrahydropteridine + O2
L-tyrosine + dihydropteridine + H2O
recombinant wild-type and mutant
-
?
L-tyrosine + (6R)-L-erythro-1',2'-dihydroxypropyltetrahydropterin + O2
?
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + (6R)-L-erythro-1',2'-dihydroxypropyltetrahydropterin + O2
?
-
-
-
-
?
L-tyrosine + (6R)-L-erythro-1',2'-dihydroxypropyltetrahydropterin + O2
?
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + (6R)-L-erythro-tetrahydrobiopterin + O2
?
-
preferred electron donor
-
-
?
L-tyrosine + (6R)-L-erythro-tetrahydrobiopterin + O2
?
-
tyrosine at 0.1 mM and O2 at 4.8% inhibit with (6R)-L-erythro-tetrahydrobiopterin as electron donor, depending on O2 and cofactor concentration
-
-
?
L-tyrosine + (6R)-L-erythro-tetrahydrobiopterin + O2
?
-
recombinant hTH1
-
-
?
L-tyrosine + (6R)-L-erythro-tetrahydrobiopterin + O2
?
-
cosubstrate has a regulatory role for all 4 isoforms
-
-
?
L-tyrosine + (6R)-L-erythro-tetrahydrobiopterin + O2
?
-
probable regulatory role of cosubstrate for all 4 isoforms
-
-
?
L-tyrosine + 2-amino-4-hydroxy-6,7-dimethyltetrahydropterin + O2
?
-
-
-
-
?
L-tyrosine + 2-amino-4-hydroxy-6,7-dimethyltetrahydropterin + O2
?
-
synthetic pterin as electron donor
-
-
?
L-tyrosine + 2-amino-4-hydroxy-6,7-dimethyltetrahydropterin + O2
?
-
synthetic pterin as electron donor
-
-
?
L-tyrosine + 2-amino-4-hydroxy-6-methyltetrahydropterin + O2
?
-
-
-
-
?
L-tyrosine + 2-amino-4-hydroxy-6-methyltetrahydropterin + O2
?
-
synthetic pterin as electron donor
-
-
?
L-tyrosine + 2-amino-4-hydroxy-6-methyltetrahydropterin + O2
?
-
-
-
-
?
L-tyrosine + 2-amino-4-hydroxy-6-methyltetrahydropterin + O2
?
-
synthetic pterin as electron donor
-
-
?
L-tyrosine + 5,6,7,8-tetrahydro-L-biopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydro-L-biopterin
-
-
-
-
?
L-tyrosine + 5,6,7,8-tetrahydro-L-biopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydro-L-biopterin
-
-
-
-
?
L-tyrosine + 5,6,7,8-tetrahydro-L-biopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydro-L-biopterin
-
-
-
-
?
L-tyrosine + 5,6,7,8-tetrahydro-L-biopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydro-L-biopterin
-
-
-
-
?
L-tyrosine + 5,6,7,8-tetrahydro-L-biopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydro-L-biopterin
-
-
-
-
?
L-tyrosine + 5,6,7,8-tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-tyrosine + 5,6,7,8-tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-tyrosine + 5,6,7,8-tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin
-
-
-
?
L-tyrosine + 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine + O2
3,4-dihydroxyphenylalanine + ?
-
-
-
-
?
L-tyrosine + 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine + O2
3,4-dihydroxyphenylalanine + ?
-
-
-
-
?
L-tyrosine + 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine + O2
3,4-dihydroxyphenylalanine + ?
-
-
-
-
?
L-tyrosine + 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine + O2
?
-
-
-
-
?
L-tyrosine + 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine + O2
?
-
-
-
-
?
L-tyrosine + 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine + O2
?
-
-
-
-
?
L-tyrosine + 6-methyltetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 6-methyl-4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-tyrosine + 6-methyltetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 6-methyl-4a-hydroxytetrahydrobiopterin
-
-
-
-
?
L-tyrosine + 6-methyltetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 6-methyl-4a-hydroxytetrahydrobiopterin
best substrate
-
-
?
L-tyrosine + 6-methyltetrahydropterin + O2
?
-
-
-
-
?
L-tyrosine + 6-methyltetrahydropterin + O2
?
-
artificial cosubstrate
-
-
?
L-tyrosine + 6-methyltetrahydropterin + O2
?
-
-
-
-
?
L-tyrosine + 6-methyltetrahydropterin + O2
?
-
higher activity than with tetrahydropterin
-
-
?
L-tyrosine + 6-methyltetrahydropterin + O2
?
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the rate-limiting enzyme in the biosynthesis of the catecholamines
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
alpha-synuclein is a negative regulator of the enzyme and the dopamine biosynthesis pathway
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
key and rate-limiting enzyme in dopamine and other catecholamine biosynthesis, regulation, mechanisms, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
key enzyme in dopamine synthesis, negative catecholamine end-product regulation, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
rate-limiting enzyme in the synthesis of catecholamine neurotransmitters, complex regulation by the cofactor including both enzyme inactivation and conformational stabilization, enzyme defects are associated with L-DOPA responsive and non-responsive dystonia and infantile parkinsonism, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
rate-limiting enzyme of the catecholamine biosynthesis
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the glial cell line-derived neurotrophic factor, GDNF, is involved in the regulation of tyrosine hydroxylase levels in the midbrain
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
tyrosine hydroxylase is the rate-limiting enzyme in catecholamine biosynthesis
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the enzyme is a major producer of the DOPA required for both cuticle tanning and immune-associated melanization, overview
i.e. L-dopa
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
rate-limiting enzyme in dopamine biosynthesis, regulation by reversible phosphorylation, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
rate-limiting enzyme in dopamine biosynthesis, tyrosine hydroxylase activity and dopamine biosynthesis are enhanced by down-regulation of alpha-synuclein. Loss of functional alpha-synuclein may result in increased dopamine levels in neurons that may lead to cell injury or even death and is involved in Parkinson's disease
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the enzyme expression is increased in ataxic mice, Cdk5 activity cannot account for abnormal tyrosine hydroxylase expression in the cerebellum
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
tyrosine hydroxylase is the rate limiting enzyme in catecholamine synthesis, and is involved in Parkinson's disease, enzyme inhibition by alpha-synuclein causes the dopaminergic phenotype, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
rate-limiting enzyme in dopamine biosynthesis, tyrosine hydroxylase activity and dopamine biosynthesis are enhanced by down-regulation of alpha-synuclein. Loss of functional alpha-synuclein may result in increased dopamine levels in neurons that may lead to cell injury or even death and is involved in Parkinson's disease
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
684367, 685885, 685887, 687055, 687935, 688519, 688523, 688528, 688545, 688624, 689074, 689215, 689999, 690099, 695599, 697761, 713957, 714205, 714239 -
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
regulation, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
enzyme ativity regulation by endothelins is mediated by the NO pathway, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
key enzyme in dopamine biosynthesis, the enzyme is involved in the survival of grafted embryonic dopamine neurons after transplantation, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
key enzyme in dopamine biosynthesis, the majority of dopamine is derived from recycling after dopamine exocytosis, but loss in dopamine leads to de novo synthesis of dopamine, due to increased enzyme activity since the feedback enzyme inhibition by dopamine is reduced, regulation, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the enzyme catalyzes the rate-limiting step in dopamine biosynthesis, enzyme inhibition in the brain leads to hypothalamic reduced dopamine and DOPAC levels and increased pituitary prolactine, while the norepinephrine levels remain unaltered, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline and adrenaline, is regulated acutely by feedback inhibition by the catecholamines and relief of this inhibition by phosphorylation of residue Ser40. Phosphorylation of Ser40 abolishes the binding of dopamine to a high affinity site on the enzyme, thereby increasing the activity of the enzyme, regulation mechanism overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
tyrosine hydroxylase is involved in dopamine biosynthesis and the rat nigrostriatal pathway, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
substrate inhibition occurs at 0.1 mM tyrosine or O2 with (6R)- and (6RS)-tetrahydrobiopterin
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
rate-limiting step in catecholamine biosynthesis
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
the enzyme shows high substrate specificity for L-tyrosine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
the enzyme shows high substrate specificity for L-tyrosine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
recombinant hTH1
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
rate-limiting step in catecholamine biosynthesis
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
the enzyme prefers L-tyrosine as a substrate over L-phenylalanine by an order of magnitude and over L-tryptophan by 25fold
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
the enzyme shows high substrate specificity for L-tyrosine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
reaction is coupled with ascorbate oxidation
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
best substrate
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
recombinant wild-type and mutant
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
rate-limiting step in catecholamine biosynthesis
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
tetrahydropterin absolutely required
3,4-dihydroxy-L-phenylalanine is identical with dopa
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
r
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
additional information
?
-
-
in nocturnal species, rhythms in tyrosine hydroxylase-containing neurons in the hypothalamus appear to be responsible for rhythms in prolactin secretion, overview
-
-
?
additional information
?
-
-
key enzyme in dopamine biosynthesis
-
-
?
additional information
?
-
-
key enzyme in dopamine biosynthesis. Tissue-specific expression of the isoenzymes generated through alternative splicing of the tyrosine hydroxylase gene is a vital step in Drosophila development
-
-
?
additional information
?
-
-
tyrosine hydroxylase stimulates GTP cyclohydrolase I activity
-
-
?
additional information
?
-
-
circulating titer of estradiol-17 beta can act differentially on the enzyme to alter catecholamineergic activity. Estradiol-17 beta may participate in the acute regulation of the enzyme by interacting with the cAMP signaling pathway
-
-
?
additional information
?
-
-
the brain enzyme is sensitive to the thyroid status. Hormone excess activates and deficiency retards the enzyme activity by midifying its kinetic function
-
-
?
additional information
?
-
-
active with diverse tetrahydropterin analogues, substituted at C6, C7 or C3, overview
-
-
?
additional information
?
-
-
under aerobic conditions can generate significant amounts of reactive oxygen species, including hydrogen peroxide and hydroxyl radicals
-
-
?
additional information
?
-
-
direct function for tyrosine hydroxylase in the melanosome via a cencerted action with tyrosinase to promote pigmentation
-
-
?
additional information
?
-
-
the enzyme catalyzes the rate-limiting step in the biosynthesis of dopmaine. The physiological effects of the mutations described in cases of autosomal recessive DOPA-responsive dystonia are primarily due to the decreased stability of the mutant proteins razher than decreases in their intrinsic activities
-
-
?
additional information
?
-
-
tyrosinase activity is modified to tyrosine hydroxylase activity via immobilization
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
4-substituted substrate analogues get hydroxylated at position 4 or 3, the latter is preferred with big-sized substituents, multiply hydroxylated products occur as well
-
-
?
additional information
?
-
-
activation of nociceptin/orphanin FQ-NOP receptor system inhibits tyrosine hydroxylase phosphorylation, dopamine synthesis and dopamine D1 receptor signaling in rat nucleus accumbens and dorsal striatum, N/OFQ preferentially inhibits phosphoSer40-enzyme in nucleus accumbens shell, overview
-
-
?
additional information
?
-
-
neuronal activity, modulated e.g. by KCl, mediates changes in TH expression, overview
-
-
?
additional information
?
-
-
postinfarct sympathetic hyperactivity differentially stimulates expression of tyrosine hydroxylase and norepinephrine transporter, in vitro stimulation of sympathetic neurons increases tyrosine hydroxylase and norepinephrine synthesis to a greater extent than it stimulates norepinephrine reuptake and the NE transporter, overview
-
-
?
additional information
?
-
-
the enzyme is not circadianally regulated by the chromaffin cell clock, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-tyrosine + (6R)-L-erythro-1',2'-dihydroxypropyltetrahydropterin + O2
?
L-tyrosine + (6R)-L-erythro-tetrahydrobiopterin + O2
?
-
probable regulatory role of cosubstrate for all 4 isoforms
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
L-tyrosine + tetrahydropteridine + O2
3,4-dihydroxyphenylalanine + dihydropteridine + H2O
-
-
-
-
?
additional information
?
-
L-tyrosine + (6R)-L-erythro-1',2'-dihydroxypropyltetrahydropterin + O2
?
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + (6R)-L-erythro-1',2'-dihydroxypropyltetrahydropterin + O2
?
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the rate-limiting enzyme in the biosynthesis of the catecholamines
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
alpha-synuclein is a negative regulator of the enzyme and the dopamine biosynthesis pathway
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
key and rate-limiting enzyme in dopamine and other catecholamine biosynthesis, regulation, mechanisms, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
key enzyme in dopamine synthesis, negative catecholamine end-product regulation, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
rate-limiting enzyme in the synthesis of catecholamine neurotransmitters, complex regulation by the cofactor including both enzyme inactivation and conformational stabilization, enzyme defects are associated with L-DOPA responsive and non-responsive dystonia and infantile parkinsonism, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
rate-limiting enzyme of the catecholamine biosynthesis
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the glial cell line-derived neurotrophic factor, GDNF, is involved in the regulation of tyrosine hydroxylase levels in the midbrain
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
tyrosine hydroxylase is the rate-limiting enzyme in catecholamine biosynthesis
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the enzyme is a major producer of the DOPA required for both cuticle tanning and immune-associated melanization, overview
i.e. L-dopa
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
rate-limiting enzyme in dopamine biosynthesis, regulation by reversible phosphorylation, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
rate-limiting enzyme in dopamine biosynthesis, tyrosine hydroxylase activity and dopamine biosynthesis are enhanced by down-regulation of alpha-synuclein. Loss of functional alpha-synuclein may result in increased dopamine levels in neurons that may lead to cell injury or even death and is involved in Parkinson's disease
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the enzyme expression is increased in ataxic mice, Cdk5 activity cannot account for abnormal tyrosine hydroxylase expression in the cerebellum
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
tyrosine hydroxylase is the rate limiting enzyme in catecholamine synthesis, and is involved in Parkinson's disease, enzyme inhibition by alpha-synuclein causes the dopaminergic phenotype, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
rate-limiting enzyme in dopamine biosynthesis, tyrosine hydroxylase activity and dopamine biosynthesis are enhanced by down-regulation of alpha-synuclein. Loss of functional alpha-synuclein may result in increased dopamine levels in neurons that may lead to cell injury or even death and is involved in Parkinson's disease
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
regulation, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
enzyme ativity regulation by endothelins is mediated by the NO pathway, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
key enzyme in dopamine biosynthesis, the enzyme is involved in the survival of grafted embryonic dopamine neurons after transplantation, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
key enzyme in dopamine biosynthesis, the majority of dopamine is derived from recycling after dopamine exocytosis, but loss in dopamine leads to de novo synthesis of dopamine, due to increased enzyme activity since the feedback enzyme inhibition by dopamine is reduced, regulation, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the enzyme catalyzes the rate-limiting step in dopamine biosynthesis, enzyme inhibition in the brain leads to hypothalamic reduced dopamine and DOPAC levels and increased pituitary prolactine, while the norepinephrine levels remain unaltered, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
the rate-limiting enzyme in the biosynthesis of the catecholamines dopamine, noradrenaline and adrenaline, is regulated acutely by feedback inhibition by the catecholamines and relief of this inhibition by phosphorylation of residue Ser40. Phosphorylation of Ser40 abolishes the binding of dopamine to a high affinity site on the enzyme, thereby increasing the activity of the enzyme, regulation mechanism overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin + H2O
-
tyrosine hydroxylase is involved in dopamine biosynthesis and the rat nigrostriatal pathway, overview
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
rate-limiting step in catecholamine biosynthesis
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
the enzyme shows high substrate specificity for L-tyrosine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
the enzyme shows high substrate specificity for L-tyrosine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
rate-limiting step in catecholamine biosynthesis
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
the enzyme prefers L-tyrosine as a substrate over L-phenylalanine by an order of magnitude and over L-tryptophan by 25fold
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
the enzyme shows high substrate specificity for L-tyrosine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
reaction is coupled with ascorbate oxidation
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
best substrate
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
first step in biosynthesis of catecholamines such as norepinephrine, epinephrine and dopamine
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
3,4-dihydroxy-L-phenylalanine + dihydrobiopterin + H2O
-
rate-limiting step in catecholamine biosynthesis
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
L-tyrosine + tetrahydrobiopterin + O2
L-dopa + 4a-hydroxytetrahydrobiopterin + H2O
-
-
-
-
?
additional information
?
-
-
in nocturnal species, rhythms in tyrosine hydroxylase-containing neurons in the hypothalamus appear to be responsible for rhythms in prolactin secretion, overview
-
-
?
additional information
?
-
-
key enzyme in dopamine biosynthesis
-
-
?
additional information
?
-
-
key enzyme in dopamine biosynthesis. Tissue-specific expression of the isoenzymes generated through alternative splicing of the tyrosine hydroxylase gene is a vital step in Drosophila development
-
-
?
additional information
?
-
-
tyrosine hydroxylase stimulates GTP cyclohydrolase I activity
-
-
?
additional information
?
-
-
circulating titer of estradiol-17 beta can act differentially on the enzyme to alter catecholamineergic activity. Estradiol-17 beta may participate in the acute regulation of the enzyme by interacting with the cAMP signaling pathway
-
-
?
additional information
?
-
-
the brain enzyme is sensitive to the thyroid status. Hormone excess activates and deficiency retards the enzyme activity by midifying its kinetic function
-
-
?
additional information
?
-
-
direct function for tyrosine hydroxylase in the melanosome via a cencerted action with tyrosinase to promote pigmentation
-
-
?
additional information
?
-
-
the enzyme catalyzes the rate-limiting step in the biosynthesis of dopmaine. The physiological effects of the mutations described in cases of autosomal recessive DOPA-responsive dystonia are primarily due to the decreased stability of the mutant proteins razher than decreases in their intrinsic activities
-
-
?
additional information
?
-
-
activation of nociceptin/orphanin FQ-NOP receptor system inhibits tyrosine hydroxylase phosphorylation, dopamine synthesis and dopamine D1 receptor signaling in rat nucleus accumbens and dorsal striatum, N/OFQ preferentially inhibits phosphoSer40-enzyme in nucleus accumbens shell, overview
-
-
?
additional information
?
-
-
neuronal activity, modulated e.g. by KCl, mediates changes in TH expression, overview
-
-
?
additional information
?
-
-
postinfarct sympathetic hyperactivity differentially stimulates expression of tyrosine hydroxylase and norepinephrine transporter, in vitro stimulation of sympathetic neurons increases tyrosine hydroxylase and norepinephrine synthesis to a greater extent than it stimulates norepinephrine reuptake and the NE transporter, overview
-
-
?
additional information
?
-
-
the enzyme is not circadianally regulated by the chromaffin cell clock, overview
-
-
?
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(6R)-L-erythro-1',2'-dihydroxypropyltetrahydropterin
-
80% inhibition when the enzyme is preincubated with (6R)-L-erythro-1',2'-dihydroxypropyltetrahydropterin. Inhibition was attenuated by simultanious addition of dopamine
(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin
-
i.e. BH4, cofactor, complex regulation by the cofactor including both enzyme inactivation and conformational stabilization, competitive inhibition, synergistically with DTT
(6S)-L-erythro-1',2'-dihydroxypropyltetrahydropterin
-
80% inhibition when the enzyme is preincubated with (6S)-L-erythro-1',2'-dihydroxypropyltetrahydropterin
1,2,3,4-tetrahydropapaveroline
-
50% inhibition at 7.5 microM
2,4-diamino-6-dihydroxypropyl-5,6,7,8-tetrahydropterin
-
competitive against (6R)-L-erythro-tetrahydrobiopterin
2-hydroxyestradiol-17beta
-
noncompetitive
3,4-dihydroxy-L-phenylalanine
3,4-dihydroxybenzoic acid
-
-
3,4-dihydroxyphenylacetaldehyde
4-[(1R)-2-amino-1-hydroxyethyl]benzene-1,2-diol
-
competitive
5(N-phenylthiocarbamoyl)-5,6,7,8-tetrahydropterin
-
-
5-Deaza-6-methyltetrahydropterin
-
-
5-methyl-5,6,7,8-tetrahydropterin
-
competitive against (6R)-L-erythro-tetrahydrobiopterin
5-[(3-azido-6-nitrobenzylidene)amino]-2,6-diamino-4-pyrimidinone
-
competitive against tetrahydrobiopterin
6-methyltetrahydropterin
-
80% inhibition when the enzyme is preincubated with 6-methyltetrahydropterin
6-[2-(4-benzoylphenyl)propionyloxymethyl]-5,6,7,8-tetrahydropterin
-
competitive against (6R)-L-erythro-tetrahydrobiopterin
7-amino-3,3a,4,5-tetrahydro-8H-2-oxa-5,6,8,9b-tetraaza-cyclopenta[a]naphthalene-1,9-dione
-
competitive against (6R)-L-erythro-tetrahydrobiopterin
8-methyl-6,7-dimethyl-5,6,7,8-tetrahydropterin
-
competitive against (6R)-L-erythro-tetrahydrobiopterin
alpha-methyl-L-tyrosine
-
in vivo injection into the neurointermediate lobe of the pituitary gland, i.e. the intracerebro-ventricular and intra-arcuatus injection, leads to reduced synthesis of dopamine and DOPA, but not of norepinephrine, and leads to increased contents of pituitary prolactin, overview
alpha-Propyldihydroxyphenylacetamide
-
-
Bathocuproine sulfonate
-
slightly
bathophenanthroline sulfonate
CoCl2
-
0.1 mM CoCl2 results in more than 80% inhibition
dihydrobiopterin
-
L-dopa-oxidase activity
DL-6-methyl-5,6,7,8-tetrahydropterine
-
3.0-4.5 mM
dopamine quinone
-
covalent modification and inactivation
DTT
-
inactivates the enzyme, synergistically with tetrahydrobiopterin
endothelin-1
-
effects of long-term modulation at different concentrations, overview
endothelin-2
-
effects of long-term modulation at different concentrations, overview
guanidine hydrochloride
-
no activity at guanidine hydrochloride concentrations exceeding 0.6 M
L-alpha-methyl-p-tyrosine
specific and potent inhibitor
L-erythro-7,8-dihydrobiopterin
-
competitive against tetrahydropterin
Mn2+
-
50% inhibition at 0.01 mM
N-methyl-norsalsolinol
-
noncompetitive with respect to L-tyrosine, N-methyl-norsalsolinol and related tetrahydroisoquinolines accumulate in the nigrostriatal system of the human brain and are increased in the cerebrospinal fluid of patients with Parkinsons disease
nociceptin/orphanin FQ-NOP receptor system
-
activation of nociceptin/orphanin FQ-NOP receptor system inhibits tyrosine hydroxylase phosphorylation, dopamine synthesis and dopamine D1 receptor signaling in rat nucleus accumbens and dorsal striatum, N/OFQ preferentially inhibits phosphoSer40-enzyme in nucleus accumbens shell, overview
-
norsalsolinol
-
N-methyl-norsalsolinol and related tetrahydroisoquinolines accumulate in the nigrostriatal system of the human brain and are increased in the cerebrospinal fluid of patients with Parkinsons disease
salsolinol
-
50% inhibition at 35.4 microM and 4.1 microM when assayed at 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine concentration of 0.5 mM or 0.25 mM, respectively
tetrahydrobiopterin
-
substrate inhibition at tyrosine and O2 concentrations higher than 0.1 mM and 2.2 mM, respectively
1,10-phenanthroline
-
-
1,10-phenanthroline
-
complete
3,4-dihydroxy-L-phenylalanine
-
product inhibition
3,4-dihydroxy-L-phenylalanine
-
incubation with 3,4-dihydroxy-L-phenylalanine results in an inhibition of tyrosine hydroxylase activity in situ under both basal conditions and conditions that promote the phosphorylation of Ser40. 3,4-dihydroxy-L-phenylalanine binding to the high affinity site alone inhibits tyrosine hydroxylase activity to approximately 15% and 24% of control (non-dopamine bound) levels at 0.02 mM and 2.0 mM 5,6,7,8-tetrahydrobiopterin, respectively
3,4-dihydroxy-L-phenylalanine
-
product inhibition
3,4-dihydroxyphenylacetaldehyde
-
potent inhibitor, 0.01 and 0.02 mM cause 66% and 75% inhibition, respectively
3,4-dihydroxyphenylacetaldehyde
-
potent inhibitor
3-iodo-L-tyrosine
-
-
3-iodo-L-tyrosine
-
complete
3-iodo-L-tyrosine
-
competitive inhibitor
adrenaline
-
-
alpha-methyl-p-tyrosine
-
-
alpha-methyl-p-tyrosine
-
complete inhibition at 0.001 mM
bathophenanthroline sulfonate
-
-
bathophenanthroline sulfonate
-
-
Catecholamines
-
feedback inhibition, reversible by phosphorylation
Catecholamines
-
e.g. dopamine, feedback inhibition, phosphorylation by protein kinase A at Ser40, the most prominent of these regulatory sites, increases the dissociation rate of bound catecholamine inhibitors
Co2+
-
-
Co2+
-
competitive against Fe2+
Co2+
-
80% inhibition at 0.1 mM
dopamine
-
-
dopamine
-
feedback inhibition, in the presence of 0.02 mM dopamine tyrosine hydroxylase enzyme specific activity is reduced by about 60%
dopamine
-
binds to the iron ion at the active site
dopamine
-
feedback inhibitor and catecholamine product, binding inhibits and stabilizes the enzyme, reversible and competitive inhibition with respect to tetrahydrobiopterin
dopamine
-
binding kinetics and regulatory function, overview, phosphorylation of Ser40 abolishes the binding of dopamine to a high affinity site on the enzyme, thereby increasing the activity of the enzyme. Binding of dopamine to the high-affinity site also decreases Vmax and increases the Km for the cofactor tetrahydrobiopterin, while binding of dopamine to the low affinity site regulates tyrosine hydroxylase activity by increasing the Km for tetrahydrobiopterin
dopamine
-
end product inhibition
dopamine
-
feedback inhibitor, competitively with tetrahydrobiopterin
dopamine
1.8% residual activity at 0.01 mM
epinephrine
-
-
epinephrine
-
feedback inhibitor
estradiol-17beta
-
biphasic effects on in vivo and in vitro enzyme activity and kinetics. Low concentrations (1 nM) stimulate, and high concentrations (1 mM) inhibit
estradiol-17beta
-
inhibiting at concetration above 0.5 mM. adenosine 3',5' cyclic monophosphate enhances the inhibition at high estradiol-17beta concentrations
L-Dopa
-
-
L-Dopa
-
above 0.15 mM inhibiting L-dopa-oxidase activity in presence of tetrahydropterin, but not with 6,7-dimethyltetrahydropterin
L-Dopa
-
modest feedback inhibition
L-Dopa
-
Increased levels of intracellular L-DOPA inhibits tyrosine hydroxylase activity by end-product inhibition at early time points, L-DOPA (20-200 microM) treatment leads to a 562%-937% increase in L-DOPA influx at 1 h, which inhibits the activity of tyrosine hydroylase during the same period.
L-phenylalanine
-
-
L-tyrosine
-
-
L-tyrosine
-
substrate inhibition at concentrations above 0.05 mM
Ni2+
-
-
Ni2+
-
competitive against Fe2+
noradrenaline
-
-
norepinephrine
-
-
norepinephrine
-
feedback inhibitor
O2
-
above 4.8%
phenylalanine
-
-
phenylalanine
-
L-isomer, not D-isomer
RNA
-
above 0.015 mg/ml
tyrosine
-
0.1 mM
tyrosine
-
substrate inhibition, with (6R)-L-erythro-tetrahydrobiopterin
tyrosine
-
at concentrations above 0.03 mM
Zn2+
-
-
Zn2+
-
competitive against Fe2+
additional information
-
pH-dependence of inhibitor binding
-
additional information
-
inhibition of cAMP-protein kinase A and protein kinase C in crude extracts significantly reduces tyrosine hydroxylase activity
-
additional information
-
no inhibition by nonhydroxylated N-methyl-1,2,3,4-tetrahydroisoquinoline
-
additional information
-
glial cell line-derived neurotrophic factor, GDNF, supresses the enzyme expression in the midbrain
-
additional information
-
phosphorylation at Ser40 activates the enzyme, the phosphorylation is inhibited by alpha-synuclein, up to 183% induced by amphetamines, the phosphorylation inhibition is inhibited by melatonin, mechanisms, overview
-
additional information
-
UO126 significantly inhibits the basal phosphorylation of Ser40 in isoform TH1, but does not inhibit the phosphorylation of Ser44 in isoform TH2
-
additional information
-
there is no significant decrease in tyrosine hydroxylase activity at 0.02 mM or 2.0 mM 5,6,7,8-tetrahydrobiopterin following ovalbumin-coated charcoal treatment
-
additional information
-
dephosphorylation of Ser40, by phosphatase PP2A, inhibits the enzyme, protein kinase Cdelta increases the inhibition by activating PP2A, and physically associates with the tyrosine hydroxylase
-
additional information
-
alpha-synuclein inhibits phosphorylation of the enzyme at Ser40 and enzyme activity, thereby regulating the dopamine level
-
additional information
-
alpha-synuclein inhibits the enzyme by inhibiting enzyme phosphorylation at Ser40 in the regulatory domain, aggregated alpha-Syn is no longer able to inhibit tyrosine hydroxylase, overview
-
additional information
-
inhibited by metal chelating agents
-
additional information
-
PD-098059, compound C, i.e. 6-[4-(2-piperidin-1-yl-ethoxy)-phenyl]-3-pyridin-4-yl-pyrrazolo[1,5-a]-pyrimidine, and 5'-amino-5'-dAdo inhibit the activation of the enzyme by AMP-activated protein kinase, PD-098059 specifically inhibits phosphorylation at Ser31 without affecting phosphorylation at Ser19 and Ser40
-
additional information
-
chronic administration of the antipsychotic drug haloperidol causes a significant increase in locomotor activity and lower levels of tyrosine hydroxylase immunoreactivity in the caudate putamen of the striatum, another drug, quetiapine, does not cause effects to the same extent and protects the cell and tyrosine hydoxylase against oxidative stress-induced damage, overview
-
additional information
-
endothelin-1 and endothelin-3 inhibit the enzyme by inhibiting enzyme phosphorylation at Ser19, Ser31, and Ser40, but the response is abolished by selective ETA and ETB antagonists BQ-610 and BQ-788, respectively. The inhibitory effect of endothelins is also reversed by Nomega-nitro-L-arginine methyl ester and 7-nitroindazole, 1H-[1,2,4]-oxadiazolo[4,3-alpha]quinozalin-1-one, and KT-5823, respectively, no inhibition of tyrosine hydroxylase by ETA and ETB selective agonists sarafotoxin S6b and IRL-1620, respectively, detailed overview
-
additional information
-
the tyrosine hydroxylase activity decreases in the hearts of rats administrated 7,12-dimethylbenz[a]anthracene + 1-isopropyl-3-methylbenzimidazole-2-selenone and 7,12-dimethylbenz[a]anthracene + 1,3-di-p-methoxybenzylpyrimidine-2-selenone according to 7,12-dimethylbenz[a]anthracene group
-
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0.023 - 0.051
(RS)-6-methyl-5,6,7,8-tetrahydropterin
0.058
2-amino-4-hydroxy-6-methyl-5,6,7,8-tetrahydropteridine
-
-
0.0001 - 0.045
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
0.34
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydropteridine
-
30°C
0.15
6-methyl-5,6,7,8-tetrahydrobiopterin
-
-
0.033 - 0.95
6-Methyl-5,6,7,8-tetrahydropterin
0.051 - 0.409
6-methyltetrahydropterin
0.0016 - 5
L-phenylalanine
0.00105 - 2.39
L-tyrosine
0.006
O2
-
below, recombinant enzyme
0.00125 - 0.3
phenylalanine
0.0041 - 0.507
tetrahydrobiopterin
0.01 - 0.63
Tetrahydropterin
1.1
tyramine
-
pH 7.0, 37°C
additional information
additional information
-
0.023
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S19E/S40E
0.028
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S8E
0.032
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S19A
0.033
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S19A
0.033
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S19E
0.034
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, wild-type enzyme
0.035
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S40A
0.035
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S40E
0.035
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S8E
0.036
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S8A
0.037
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S19E
0.037
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S19E/S40E
0.037
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S40E
0.039
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S8A
0.04
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, wild-type enzyme
0.045
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S40A
0.047
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S31E
0.048
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S31A
0.051
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S31A
0.051
(RS)-6-methyl-5,6,7,8-tetrahydropterin
-
pH 7.0, 30°C, mutant enzyme S31E
0.0001
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
telencephalon extract, 10 microM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00015
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
telencephalon extract, 1 microM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.0002
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
hypothalamus extract, 10 microM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.0002
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
telencephalon extract, 1 nM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00022
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
hypothalamus extract, 1 nM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00024
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
hypothalamus extract, 1 microM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00024
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
telencephalon extract, 1 fM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00026
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
hypothalamus extract, 1 fM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00034
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
hypothalamus extract, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00035
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
telencephalon extract, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00045
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
hypothalamus extract, 0.01 mM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00048
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
telencephalon extract, 0.01 mM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00054
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
telencephalon extract, 1 mM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.00058
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
hypothalamus extract, 1 mM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C
0.045
6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine
-
0.1 mM L-tyrosine, 0.1 mg/ml catalase, 50 mM HEPES pH 7.0, 0.01 mM ferrous ammonium sulfate, 1 mM dithiothreitol, 25°C
0.033
6-Methyl-5,6,7,8-tetrahydropterin
recombinant wild-type, pH 7.1
0.055
6-Methyl-5,6,7,8-tetrahydropterin
recombinant wild-type, pH 6.0
0.059
6-Methyl-5,6,7,8-tetrahydropterin
recombinant mutant Y371F, pH 7.1
0.06 - 0.1
6-Methyl-5,6,7,8-tetrahydropterin
-
-
0.065
6-Methyl-5,6,7,8-tetrahydropterin
recombinant mutant Y371F, pH 6.0
0.95
6-Methyl-5,6,7,8-tetrahydropterin
-
-
0.051
6-methyltetrahydropterin
-
pH 7.1, 25°C, wild-type enzyme
0.19
6-methyltetrahydropterin
-
pH 7.1, 25°C, mutant enzyme H336E
0.339
6-methyltetrahydropterin
-
pH 7.1, 25°C, mutant enzyme H331E
0.409
6-methyltetrahydropterin
-
pH 7.1, 25°C, mutant enzyme H336Q
0.056
L-Dopa
-
recombinant hTH1, dopa-oxidase activity with tetrahydropterin
0.146
L-Dopa
-
recombinant, dopa-oxidase activity with 6,7-dimethyltetrahydropterin
0.0016
L-phenylalanine
mutant enzyme D425T, in 50 mM HEPES (pH 7.0), at 30°C
0.0053
L-phenylalanine
mutant enzyme D425G, in 50 mM HEPES (pH 7.0), at 30°C
0.0092
L-phenylalanine
mutant enzyme D425S, in 50 mM HEPES (pH 7.0), at 30°C
0.0105
L-phenylalanine
mutant enzyme D425Y, in 50 mM HEPES (pH 7.0), at 30°C
0.0144
L-phenylalanine
mutant enzyme D425F, in 50 mM HEPES (pH 7.0), at 30°C
0.0148
L-phenylalanine
mutant enzyme D425V, in 50 mM HEPES (pH 7.0), at 30°C
0.0152
L-phenylalanine
mutant enzyme D425C, in 50 mM HEPES (pH 7.0), at 30°C
0.0164
L-phenylalanine
mutant enzyme D425M, in 50 mM HEPES (pH 7.0), at 30°C
0.019
L-phenylalanine
mutant enzyme D425L, in 50 mM HEPES (pH 7.0), at 30°C
0.021
L-phenylalanine
mutant enzyme D425A, in 50 mM HEPES (pH 7.0), at 30°C
0.022
L-phenylalanine
mutant enzyme D425I, in 50 mM HEPES (pH 7.0), at 30°C
0.028
L-phenylalanine
mutant enzyme D425R, in 50 mM HEPES (pH 7.0), at 30°C
0.045
L-phenylalanine
mutant enzyme D425E, in 50 mM HEPES (pH 7.0), at 30°C
0.0565
L-phenylalanine
mutant enzyme D425Q, in 50 mM HEPES (pH 7.0), at 30°C
0.062
L-phenylalanine
mutant enzyme D425N, in 50 mM HEPES (pH 7.0), at 30°C
0.1
L-phenylalanine
wild type enzyme, in 50 mM HEPES (pH 7.0), at 30°C
0.2
L-phenylalanine
mutant enzyme D425K, in 50 mM HEPES (pH 7.0), at 30°C
5
L-phenylalanine
mutant enzyme D425H, in 50 mM HEPES (pH 7.0), at 30°C
0.051
L-Tyr
-
pH 7.1, 25°C, wild-type enzyme
0.311
L-Tyr
-
pH 7.1, 25°C, mutant enzyme H336Q
0.33
L-Tyr
-
pH 7.1, 25°C, mutant enzyme H336E
0.00105
L-tyrosine
mutant enzyme D425T, in 50 mM HEPES (pH 7.0), at 30°C
0.005
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S31A, cosubstrate 0.3 mM tetrahydropterin
0.006
L-tyrosine
mutant enzyme D425L, in 50 mM HEPES (pH 7.0), at 30°C
0.0069
L-tyrosine
mutant enzyme D425M, in 50 mM HEPES (pH 7.0), at 30°C
0.008
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S31E, cosubstrate 0.3 mM tetrahydropterin
0.0081
L-tyrosine
mutant enzyme R37E/R38E, pH and temperature not specified in the publication
0.0089
L-tyrosine
mutant enzyme D425S, in 50 mM HEPES (pH 7.0), at 30°C
0.009
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S19A, cosubstrate 0.3 mM tetrahydropterin
0.009
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S19E, cosubstrate 0.3 mM tetrahydropterin
0.009
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S19E/S40E, cosubstrate 0.3 mM tetrahydropterin
0.009
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S40E, cosubstrate 0.3 mM tetrahydropterin
0.009
L-tyrosine
-
pH 7.0, 30°C, wild-type enzyme, cosubstrate 0.3 mM tetrahydropterin
0.01
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S40A, cosubstrate 0.3 mM tetrahydropterin
0.0106
L-tyrosine
mutant enzyme D425G, in 50 mM HEPES (pH 7.0), at 30°C
0.011
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S8A, cosubstrate 0.3 mM tetrahydropterin
0.011
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S8E, cosubstrate 0.3 mM tetrahydropterin
0.014
L-tyrosine
mutant enzyme K366L, pH and temperature not specified in the publication
0.015
L-tyrosine
mutant enzyme D425C, in 50 mM HEPES (pH 7.0), at 30°C
0.015
L-tyrosine
mutant enzyme E362R/E365R, pH and temperature not specified in the publication
0.016
L-tyrosine
wild type enzyme, pH and temperature not specified in the publication
0.016
L-tyrosine
mutant enzyme D361N, pH and temperature not specified in the publication
0.016
L-tyrosine
mutant enzyme E362G, pH and temperature not specified in the publication
0.017
L-tyrosine
-
0-0.4 mM L-tyrosine, 1 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, 200 mM Na-HEPES pH 7.0, 100 mM 2-mercaptoethanol, 0.2 mg/ml catalase, 37°C
0.0172
L-tyrosine
mutant enzyme D425F, in 50 mM HEPES (pH 7.0), at 30°C
0.0187
L-tyrosine
mutant enzyme D425H, in 50 mM HEPES (pH 7.0), at 30°C
0.019
L-tyrosine
mutant enzyme E365G, pH and temperature not specified in the publication
0.02
L-tyrosine
mutant enzyme A297L, pH and temperature not specified in the publication
0.024
L-tyrosine
-
W166F/W233F/W372F/F14W mutant protein, pH 7, 25°C
0.025
L-tyrosine
mutant enzyme S368A, pH and temperature not specified in the publication
0.026
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S19E, cosubstrate 0.4 mM 6-methyltetrahydropterin
0.0263
L-tyrosine
-
recombinant wild type enzyme, at pH 7.5 and 37°C
0.029
L-tyrosine
-
native wild type enzyme, at pH 7.5 and 37°C
0.03
L-tyrosine
mutant enzyme Y423A, in 50 mM HEPES (pH 7.0), at 30°C
0.0308
L-tyrosine
mutant enzyme D425Y, in 50 mM HEPES (pH 7.0), at 30°C
0.035
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S19A, cosubstrate 0.4 mM 6-methyltetrahydropterin
0.039
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme T283M
0.04
L-tyrosine
-
wild type protein, pH 7, 25°C
0.04
L-tyrosine
mutant enzyme D425V, in 50 mM HEPES (pH 7.0), at 30°C
0.04
L-tyrosine
wild type enzyme, in 50 mM HEPES (pH 7.0), at 30°C
0.041
L-tyrosine
-
pH 7.0, 30°C, wild-type enzyme, cosubstrate 0.4 mM 6-methyltetrahydropterin
0.041
L-tyrosine
mutant enzyme D425I, in 50 mM HEPES (pH 7.0), at 30°C
0.042
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme R306H
0.042
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S8A, cosubstrate 0.4 mM 6-methyltetrahydropterin
0.0428
L-tyrosine
-
mutant enzyme E434A, at pH 7.5 and 37°C
0.043
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme T463M
0.043
L-tyrosine
-
W166F/W233F/W372F/F74W mutant protein, pH 7, 25°C
0.044
L-tyrosine
mutant enzyme Q424A, in 50 mM HEPES (pH 7.0), at 30°C
0.046
L-tyrosine
-
pH 7.0, 30°C, wild-type enzyme
0.046
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S40A, cosubstrate 0.4 mM 6-methyltetrahydropterin
0.047
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S40E, cosubstrate 0.4 mM 6-methyltetrahydropterin
0.047
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S8E, cosubstrate 0.4 mM 6-methyltetrahydropterin
0.051
L-tyrosine
mutant enzyme T427A, in 50 mM HEPES (pH 7.0), at 30°C
0.053
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S31E, cosubstrate 0.4 mM 6-methyltetrahydropterin
0.055
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S31A, cosubstrate 0.4 mM 6-0.053 methyltetrahydropterin
0.056
L-tyrosine
mutant enzyme D425A, in 50 mM HEPES (pH 7.0), at 30°C
0.058
L-tyrosine
-
W166F/W233F/W372F/F34W mutant protein, pH 7, 25°C
0.059
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme S19E/S40E, cosubstrate 0.4 mM 6-methyltetrahydropterin
0.066
L-tyrosine
-
pH 7.0, 30°C, mutant enzyme T245P
0.066
L-tyrosine
mutant enzyme Q426A, in 50 mM HEPES (pH 7.0), at 30°C
0.08
L-tyrosine
-
0.38 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, 0.1 mg/ml catalase, 50 mM HEPES pH 7.0, 0.01 mM ferrous ammonium sulfate, 1 mM dithiothreitol, 25°C
0.088
L-tyrosine
mutant enzyme D425R, in 50 mM HEPES (pH 7.0), at 30°C
0.097
L-tyrosine
mutant enzyme D425E, in 50 mM HEPES (pH 7.0), at 30°C
0.162
L-tyrosine
mutant enzyme D425Q, in 50 mM HEPES (pH 7.0), at 30°C
0.172
L-tyrosine
mutant enzyme D425N, in 50 mM HEPES (pH 7.0), at 30°C
0.8086
L-tyrosine
-
pH 6.0, 37°C
2.39
L-tyrosine
mutant enzyme D425K, in 50 mM HEPES (pH 7.0), at 30°C
0.00125
phenylalanine
recombinant mutant D425V
0.0077
phenylalanine
recombinant mutant H323Y
0.0088
phenylalanine
recombinant mutant Q310H
0.01
phenylalanine
recombinant mutant Y371F
0.1
phenylalanine
recombinant wild-type
0.11
phenylalanine
recombinant wild-type
0.3
phenylalanine
-
bovine adrenal
0.0041
tetrahydrobiopterin
-
pH 7.0, 37°C
0.0056
tetrahydrobiopterin
wild type, phosphorylated protein, pH 7.2, 30°C
0.0068
tetrahydrobiopterin
wild type protein, dopamine bound but removed from low-affinity site, pH 7.2, 30°C
0.0072
tetrahydrobiopterin
E332D phosphorylated mutant protein, pH 7.2, 30°C
0.0083
tetrahydrobiopterin
E332D mutant protein, pH 7.2, 30°C
0.009
tetrahydrobiopterin
-
pH 7.0, 30°C, mutant enzyme T463M
0.0099
tetrahydrobiopterin
L294Y phosphorylated mutant protein, pH 7.2, 30°C
0.01
tetrahydrobiopterin
-
pH 7.0, 30°C, mutant enzyme R306H
0.01
tetrahydrobiopterin
-
pH 7.0, 30°C, mutant enzyme T283M
0.012
tetrahydrobiopterin
F300Y phosphorylated mutant protein, pH 7.2, 30°C
0.013
tetrahydrobiopterin
-
pH 7.0, 30°C, wild-type enzyme
0.014
tetrahydrobiopterin
-
pH 7.0, 30°C, mutant enzyme T245P
0.014
tetrahydrobiopterin
L294A mutant protein, pH 7.2, 30°C
0.014
tetrahydrobiopterin
wild type protein, pH 7.2, 30°C
0.015
tetrahydrobiopterin
L294Y mutant protein, pH 7.2, 30°C
0.017
tetrahydrobiopterin
A297L phosphorylated mutant protein, pH 7.2, 30°C
0.017
tetrahydrobiopterin
Y371F mutant protein, pH 7.2, 30°C
0.02
tetrahydrobiopterin
A297L mutant protein, pH 7.2, 30°C
0.026
tetrahydrobiopterin
F300Y mutant protein, pH 7.2, 30°C
0.027
tetrahydrobiopterin
A297L mutant protein, dopamine bound to the high-affinity site, pH 7.2, 30°C
0.027
tetrahydrobiopterin
Y371F mutant protein, dopamine bound to the high-affinity site, pH 7.2, 30°C
0.029
tetrahydrobiopterin
L294A phosphorylated mutant protein, pH 7.2, 30°C
0.029
tetrahydrobiopterin
Y371F phosphorylated mutant protein, pH 7.2, 30°C
0.034
tetrahydrobiopterin
E332D mutant protein, dopamine bound to the high-affinity site, pH 7.2, 30°C
0.04
tetrahydrobiopterin
-
wild type protein, pH 7, 25°C
0.0426
tetrahydrobiopterin
-
pH 6.9, 37°C
0.045
tetrahydrobiopterin
-
-
0.0471
tetrahydrobiopterin
-
native wild type enzyme, at pH 7.5 and 37°C
0.0519
tetrahydrobiopterin
-
recombinant wild type enzyme, at pH 7.5 and 37°C
0.054
tetrahydrobiopterin
F300A mutant protein, pH 7.2, 30°C
0.055
tetrahydrobiopterin
-
W166F/W233F/W372F/F14W mutant protein, pH 7, 25°C
0.065
tetrahydrobiopterin
-
W166F/W233F/W372F/F74W mutant protein, pH 7, 25°C
0.07
tetrahydrobiopterin
F300A phosphorylated mutant protein, pH 7.2, 30°C
0.077
tetrahydrobiopterin
-
W166F/W233F/W372F/F34W mutant protein, pH 7, 25°C
0.134
tetrahydrobiopterin
wild type protein, dopamine bound to the high-affinity site, pH 7.2, 30°C
0.341
tetrahydrobiopterin
-
mutant enzyme E434A, at pH 7.5 and 37°C
0.356
tetrahydrobiopterin
wild type protein, in the presence of dopamine, pH 7.2, 30°C
0.507
tetrahydrobiopterin
wild type, phosphorylated protein, in the presence of dopamine, pH 7.2, 30°C
0.01
Tetrahydropterin
-
recombinant phosphorylated hTH1, L-dopa-oxidase activity
0.021
Tetrahydropterin
-
recombinant enzyme, value is pH-dependent
0.027
Tetrahydropterin
recombinant wild-type, pH 7.1
0.053
Tetrahydropterin
recombinant mutant Y371F, pH 7.1
0.08
Tetrahydropterin
-
low Km form
0.63
Tetrahydropterin
-
high Km form
0.0061
tyrosine
-
-
0.0094
tyrosine
-
recombinant enzyme, pH-independent
0.016
tyrosine
recombinant wild-type
0.032
tyrosine
recombinant wild-type, pH 6.0
0.045
tyrosine
recombinant mutant D425V
0.05
tyrosine
-
bovine adrenal gland
0.051
tyrosine
recombinant wild-type, pH 7.1
0.054
tyrosine
recombinant mutant Q310H
0.055
tyrosine
-
recombinant isoform hTH2, with 6-methyltetrahydropterin
0.065
tyrosine
recombinant mutant Y371F, pH 7.1
0.066
tyrosine
-
recombinant isoform hTH4, with 6-methyltetrahydropterin
0.071
tyrosine
recombinant mutant Y371F, pH 6.0
0.074
tyrosine
-
recombinant isoform hTH3, with 6-methyltetrahydropterin
0.075
tyrosine
-
with 6-methyltetrahydropterin
0.092
tyrosine
recombinant mutant H323Y
0.166
tyrosine
-
recombinant isoform hTH1, with 6-methyltetrahydropterin
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
Km-values of diverse tetrahydropterin analogues, substituted at C6, C7 or C3
-
additional information
additional information
-
phosphorylation converts the enzyme from a form possessing a high Km for pterin cofactor to a form with a low Km for pterin cofactor
-
additional information
additional information
-
effect of RNA on Km
-
additional information
additional information
-
effect of RNA on Km
-
additional information
additional information
-
rat brain: 2 kinetically distinguishable forms: low Km form, high Km form
-
additional information
additional information
-
rat brain: 2 kinetically distinguishable forms: low Km form, high Km form
-
additional information
additional information
-
Km is dependent on substrate and cofactor concentration when (6R)-L-erythro-tetrahydrobiopterin is used due to inhibitory effects
-
additional information
additional information
-
Km dependence on substrate concentrations
-
additional information
additional information
-
Km dependence on substrate concentrations
-
additional information
additional information
Km-values for tyrosine of mutant phenylalanine hydroxylase with tyrosine hydroxylation activity
-
additional information
additional information
-
Km dependent on cosubstrate type and concentration, overview for 4 isoforms
-
additional information
additional information
-
both the cofactor (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin and the feedback inhibitor dopamine increase the kinetic stability of human isozyme 1 in vitro
-
additional information
additional information
-
kinetics analysis, overview
-
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E434A
-
the mutant shows 35.6% of wild type activity. Furthermore, the mutation dramatically reduces its substrate affinity for tetrahydrobiopterin and decreases its activation by Fe2+
D361N
reductions in Vmax are not significantly different from the wild type enzyme
E332A
-
the mutant has 10fold higher Km for 6-methyltetrahydropterin, but reduction of the enzyme by 6-methyltetrahydropterin is similar to the wild type
E332D
active site residue, 10fold reduction in activity, close to the catalytic iron
E332Q
active site residue, no activity, close to the catalytic iron
E362G
the Vmax is reduced compared to the wild type enzyme
E362Q
reductions in Vmax are not significantly different from the wild type enzyme
E362R/E365R
the Vmax is significantly less reduced by dopamine than for the wild type enzyme
E365G
the Vmax is reduced compared to the wild type enzyme
E365Q
the Vmax is significantly less reduced by dopamine than for the wild type enzyme
F184W/W372F
-
4fold lower Km for L-tyrosine compared to the wild-type enzyme. Similar Km for 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine compared to wild-type enzyme
F300A
active site residue
F300Y
active site residue
K170E/L480A
the mutant is inhibited over the same range of dopamine like the wild type enzyme
K366L
reductions in Vmax are not significantly different from the wild type enzyme
L294A
protrudes into catalytic cleft
L294Y
protrudes into catalytic cleft
Q381K
-
the mutation is associated with tyrosine hydroxylase deficiency
R202H
-
the mutation is associated with tyrosine hydroxylase deficiency
R233H
-
the mutation is associated with tyrosine hydroxylase deficiency
R306H
-
1.2fold decrease in Km-value for L-tyrosine compared to wild-type enzyme, Ki-value for L-tyrosine is nearly identical to wild-type value, 1.3fold decrease in KM-value for tetrahydrobiopterin compared to wild-type enzyme, 1.2fold increase of turnover-number compared to wild-type enzyme. 8.2°C increase in Tm-value compared to wild-type enzyme
R306H/T463M
-
all of the TyrH is insoluble and no enzyme can be purified
S31A
-
the mutant is not phosphorlyated
S31E
-
phospho-mimic mutant
S368A
the Vmax is significantly less reduced by dopamine than for the wild type enzyme
S40E
-
the mutant mimics a phosphorylation of S40. The kinetics of reduction and oxidation of the enzyme are similar to the wild type
T245P
-
1.4fold increase in Km-value for L-tyrosine compared to wild-type enzyme, 1.6fold increase in Ki-value for L-tyrosine compared to wild-type enzyme, 1.1fold increase in KM-value for tetrahydrobiopterin compared to wild-type enzyme, 1.6fold increase of turnover-number compared to wild-type enzyme. 3.9°C increase in Tm-value compared to wild-type enzyme
T245P/T283M
-
all of the TyrH is insoluble and no enzyme can be purified
T283M
-
1.2fold decrease in Km-value for L-tyrosine compared to wild-type enzyme, 1.2fold decrease in Ki-value for L-tyrosine compared to wild-type enzyme, 1.3fold decrease in KM-value for tetrahydrobiopterin compared to wild-type enzyme, 4.2fold decrease of turnover-number compared to wild-type enzyme
T463M
-
1.1fold decrease in Km-value for L-tyrosine compared to wild-type enzyme, Ki-value for L-tyrosine is nearly identical to wild-type value compared to wild-type enzyme, 1.4fold decrease in KM-value for tetrahydrobiopterin compared to wild-type enzyme, 1.2fold increase of turnover-number compared to wild-type enzyme. 7.7°C increase in Tm-value compared to wild-type enzyme
W166F/F184W/W233F/W372F
-
mutant protein contains one tryptophan at residue 184 in the middle of a mobile active-site loop. The mutant was generated to perform steady-state fluorescence anisotropy measurements and shows kinetic properties similar to the wild-type enzyme
W166F/F184W/W372F
-
Km for L-tyrosine similar to the wild-type enzyme. 3fold higher Km for 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine compared to wild-type enzyme
W166F/W233F/W372F
-
Km for L-tyrosine similar to the wild-type enzyme. 4fold higher Km for 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine compared to wild-type enzyme
W166F/W372F
-
Km for L-tyrosine similar to the wild-type enzyme. 3fold higher Km for 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine compared to wild-type enzyme
W372F
-
10fold lower Km for L-tyrosine compared to the wild-type enzyme. Similar Km for 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine compared to wild-type enzyme
Y371F
active site residue, close to the catalytic iron
A297L
the mutation mediates high affinity dopamine inhibition through Vmax reduction and increasing the Km value for the cofactor
D361N
the mutant shows increased Vmax compared to the wild type enzyme
D425A
the mutant shows strongly reduced activity compared to the wild type enzyme
D425C
the mutant shows strongly reduced activity compared to the wild type enzyme
D425E
the mutant shows strongly reduced activity compared to the wild type enzyme
D425F
the mutant shows strongly reduced activity compared to the wild type enzyme
D425G
the mutant shows strongly reduced activity compared to the wild type enzyme
D425H
the mutant shows strongly reduced activity compared to the wild type enzyme
D425I
the mutant shows strongly reduced activity compared to the wild type enzyme
D425K
the mutant shows strongly reduced activity compared to the wild type enzyme
D425L
the mutant shows strongly reduced activity compared to the wild type enzyme
D425M
the mutant shows strongly reduced activity compared to the wild type enzyme
D425N
the mutant shows strongly reduced activity compared to the wild type enzyme
D425Q
the mutant shows strongly reduced activity compared to the wild type enzyme
D425R
the mutant shows strongly reduced activity compared to the wild type enzyme
D425S
the mutant shows strongly reduced activity compared to the wild type enzyme
D425T
the mutant shows strongly reduced activity compared to the wild type enzyme
D425Y
the mutant shows strongly reduced activity compared to the wild type enzyme
DELTA1-120
-
not inhibited by dopamine
DELTA1-32
-
90% inhibited by dopamine
DELTA1-68
-
not inhibited by dopamine
DELTA1-76
-
not inhibited by dopamine
E332A
-
the E332A mutant hydroxylates less than 1% L-tyrosine compared to wild type and does not produce 4a-hydroxytetrahydrobiopterin
E362Q
the mutant shows reduced Vmax compared to the wild type enzyme
E362R/E365R
the mutation mediates high affinity dopamine inhibition through Vmax reduction and increasing the Km value for the cofactor
E365Q
the mutant shows reduced Vmax compared to the wild type enzyme
E376H
-
iron content is not significantly altered. Pterin oxidation at 1.2% of the wild-type activity. Tyrosine hydroxylation is less than 0.4% of the wild-type value
E376Q
-
iron content is not significantly altered. Pterin oxidation at 0.4% of the wild-type activity. Tyrosine hydroxylation is 0.39% of the wild-type value
H323Y
enhanced Km for tyrosine, 4.5fold enhanced phenylalanine hydroxylation activity, active site mutant
H331E
-
iron content is not significantly altered
H331E/E376H
-
mutant enzyme contains significantly less iron than the wild-type enzyme. Pterin oxidation at 0.21% of the wild-type activity. Tyrosine hydroxylation is less than 0.4% of the wild-type value
H331Q
-
mutant enzyme is not successfully expressed. Pterin oxidation at 2.4% of the wild-type activity. Tyrosine hydroxylation is less than 0.002% of the wild-type value
H336E
-
significant decrease in iron content. Pterin oxidation at 6.3% of the wild-type activity. Tyrosine hydroxylation is 0.78% of the wild-type value
H336Q
-
iron-free mutant enzyme. Pterin oxidation at 11.9% of the wild-type activity. Tyrosine hydroxylation is 3.7% of the wild-type value
K366L
the mutant shows reduced Vmax compared to the wild type enzyme
Q310H
4fold reduced tyrosine hydroxylation/dopa formation activity, slightly enhanced phenylalanine hydroxylation activity, active site mutant
Q424A
the mutant shows reduced activity compared to the wild type enzyme
Q426A
the mutant strongly reduced activity compared to the wild type enzyme
R37E/R38E
the Km value for tetrahydrobiopterin measured for the mutant is approximately half that of the wild type enzyme
S31A
the mutant is not phosphorlyated
S368A
the mutation mediates high affinity dopamine inhibition through Vmax reduction and increasing the Km value for the cofactor
S395A
-
the S395A mutant produces 4a-hydroxytetrahydrobiopterin at the same rate as wild type, but does so in predominantly uncoupled reaction (2% of wild type enzyme L-tyrosine hydroxylation)
T427A
the mutant shows reduced activity compared to the wild type enzyme
W166F/W233F/W372F
-
tryptophan-free enzyme with wild-type activity
W166F/W233F/W372F/F14W
-
introduced tryptophan residue in regulatory domain
W166F/W233F/W372F/F34W
-
introduced tryptophan residue in regulatory domain
W166F/W233F/W372F/F74W
-
introduced tryptophan residue in regulatory domain
Y371F
increased Km for tyrosine and pterin cosubstrates, highly decreased Km for phenylalanine
Y423A
the mutant shows reduced activity compared to the wild type enzyme
A297L
outer edge of the active site
A297L
the Vmax is significantly less reduced by dopamine than for the wild type enzyme
L205P
-
the mutant is associated with recessively inherited L-DOPA-responsive infantile parkinsonism, the mutation reduces the activity and stability of the protein in cells and in vitro expression systems, being considered a misfolding mutation
L205P
-
the mutation is associated with tyrosine hydroxylase deficiency
R37E/R38E
-
the point mutation increases the binding capacity of 5,6,7,8,-tetrahydrobiopterin to tyrosine hydroxylase molecule to increase the activity and possibly to increase the stability
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
D425V
335fold reduced tyrosine hydroxylation/dopa formation activity, 120fold reduced reaction velocity with tyrosine, 3fold enhanced phenylalanine hydroxylation activity, active site mutant
D425V
the mutant shows strongly reduced activity compared to the wild type enzyme
S19E
-
similar steady-state parameters and similar binding affinity for catecholamines to wild-type enzyme. Inactivated 1.8fold slower than the wild-type enzyme at 42°C in presence of 2% glycerol
S19E
-
mimics phosphorylation at S19
S19E
-
investigation of regulation by phosphorylation
S19E/S40E
-
mimics phosphorylation at S19S40
S19E/S40E
-
investigation of regulation by phosphorylation, slight decrease in KM value for tetrahydrobiopterin, slight increase in Vmax value
S31E
-
similar steady-state parameters and similar binding affinity for catecholamines to wild-type enzyme. Inactivated 1.8fold slower than the wild-type enzyme at 42°C in presence of 2% glycerol
S31E
-
mimics phosphorylation at S31
S31E
-
good mimic of phosphorylated wild type protein
S31E
phospho-mimic mutant
S40E
-
inactivated 1.6fold faster than the wild-type enzyme at 42°C in presence of 2% glycerol
S40E
-
mimics phosphorylation at S40
S40E
-
good mimic of phosphorylated wild type protein
S8E
-
similar steady-state parameters and similar binding affinity for catecholamines to wild-type enzyme. More stable than wild-type enzyme at 42°C in presence of 2% glycerol
S8E
-
mimics phosphorylation at S8
S8E
-
investigation of regulation by phosphorylation
additional information
-
truncated hTH1 isoform lacking the 150 N-terminal amino acids
additional information
-
construction of a truncation enzyme mutant lacking exons 2, 8, and 9 and showing reduced enzyme activity
additional information
-
detection of single nucleotide polymorphisms in the local genomic region, systematic polymorphism discovery at the TH locus and analysis for contributions to sympathetic function and blood pressure, i.e. 4 common TH promoter polymorphisms C-824T, G-801C, A-581G, and G-494A, overview
additional information
-
deletion of the N-terminus of tyrosine hydroxylase removes the high affinity dopamine binding site, but does not affect dopamine binding to the low affinity site
additional information
-
the deletion mutation of N-terminal 38-amino acids increases the binding capacity of 5,6,7,8,-tetrahydrobiopterin to tyrosine hydroxylase molecule to increase the activity and possibly to increase the stability
additional information
-
construction of neurokinin 3 receptor knockout mice, the mutant mice do not show altered tyrosine hydroxylase levels in the caudate putamen or nucleus accumbens, but show decreased enzyme levels in the olfactory tuberculum, phenotype, overview
additional information
-
increased TH-Ser40 phosphorylation in primary mesencephalic dopaminergic neurons from PKCdelta knock-out mice, overview
additional information
-
reduction of high-level tyrosine hydroxylase dopaminergic alpha-Syn-deficient cells by infection with wild-type alpha-Syn human lentivirus, overview
additional information
-
silencing alpha-synuclein gene expression by short hairpin RNA expression does not affect tyrosine hydroxylase expression but enhance tyrosine hydroxylase activity in MN9D cells by increasing TH Ser40 phosphorylation, overview
additional information
-
the pogo/pogo mouse phenotype of ataxic mice shows upregulation of tyrosine hydroxylase expression induced by enzyme phosphorylation via cyclin-dependent kinase 5, reduced Cdk5 activity in both p35-/- and p39-/- cerebellum do not correspond to defects in tyrosine hydroxylase expression, overview
additional information
-
silencing alpha-synuclein gene expression by short hairpin RNA expression does not affect tyrosine hydroxylase expression but enhance tyrosine hydroxylase activity in MN9D cells by increasing TH Ser40 phosphorylation, overview
-
additional information
active site mutants of phenylalanine hydroxylase lead to highly increased tyrosine hydroxylation activity of the enzyme mutants
additional information
-
investigation of the role of several amino acid residues in binding of substrate and ligands by site-specific mutagenesis
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