1.14.16.2: tyrosine 3-monooxygenase
This is an abbreviated version!
For detailed information about tyrosine 3-monooxygenase, go to the full flat file.
Word Map on EC 1.14.16.2
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1.14.16.2
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dopamine
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dopaminergic
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parkinsonism
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nigra
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striatum
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catecholamine
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substantia
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nerve
-
ventral
-
fiber
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sympathetic
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innervation
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adrenal
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noradrenergic
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neurotransmitter
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6-hydroxydopamine
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ganglia
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th-positive
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catecholaminergic
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neuropeptide
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norepinephrine
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nigrostriatal
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midbrain
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monoamine
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neurotrophic
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compacta
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coeruleus
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hypothalamus
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tegmental
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mesencephalic
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1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
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l-dopa
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6-ohda
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neurochemical
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accumbens
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noradrenaline
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rostrally
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dopac
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apomorphine
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perikarya
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intrastriatal
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beta-hydroxylase
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mptp-induced
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varicosity
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ventrolateral
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dopamine-beta-hydroxylase
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preoptic
-
npy
-
phenylethanolamine
-
analysis
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diagnostics
-
homovanillic
-
synthesis
- 1.14.16.2
- dopamine
-
dopaminergic
- parkinsonism
- nigra
- striatum
- catecholamine
-
substantia
- nerve
-
ventral
- fiber
-
sympathetic
-
innervation
- adrenal
-
noradrenergic
-
neurotransmitter
- 6-hydroxydopamine
- ganglia
-
th-positive
-
catecholaminergic
-
neuropeptide
- norepinephrine
-
nigrostriatal
- midbrain
-
monoamine
-
neurotrophic
- compacta
- coeruleus
- hypothalamus
- tegmental
-
mesencephalic
- 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine
- l-dopa
-
6-ohda
-
neurochemical
- accumbens
- noradrenaline
-
rostrally
-
dopac
- apomorphine
- perikarya
-
intrastriatal
- beta-hydroxylase
-
mptp-induced
-
varicosity
-
ventrolateral
- dopamine-beta-hydroxylase
-
preoptic
- npy
- phenylethanolamine
- analysis
- diagnostics
-
homovanillic
- synthesis
Reaction
Synonyms
CAT-2, DTH1, DTH2, hTH2, L-tyrosine hydroxylase, monophenol monooxygenase, oxygenase, tyrosine 3-mono-, TH, TH1, TH2, TyrH, tyrosinase, tyrosine 3-hydroxylase, tyrosine 3-monooxygenase, tyrosine hydroxylase, tyrosine hydroxylase type 1, tyrosine-3-mono-oxygenase, tyrosine-3-monooxygenase
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 1.14.16.2 - tyrosine 3-monooxygenase
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no glycoprotein
phosphoprotein
additional information
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the enzyme is phospbhorylated at Ser19, Ser31, and Ser40 and thereby activated, the activation is completely blocked by EGTA
phosphoprotein
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the enzyme is phosphorylated at Ser35 by cAMP-dependent protein kinase
phosphoprotein
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the enzyme is phosphorylated at Ser35 by cAMP-dependent protein kinase
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phosphoprotein
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the enzyme is activated by cAMP-dependent protein kinase in vitro
phosphoprotein
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activation through phosphorylation of tyrosine hydroxylase by cyclic AMP-dependent protein kinase A, inhibited in the presence of H89
phosphoprotein
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enzyme activation by reversible phosphorylation, phosphorylation by protein kinase A at Ser40, the most prominent of these regulatory sites, increases the dissociation rate of bound catecholamine feedback inhibitors
phosphoprotein
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phosphorylation at Ser40 activates the enzyme, the phosphorylationis inhibited by alpha-synuclein, up to 183% induced by amphetamines, the phosphorylation inhibition is inhibited by melatonin, mechanisms, overview
phosphoprotein
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phosphorylation of Ser40 directly increases tyrosine hydroxylase activity by inducing a 500fold increase in the rate of dissociation of the catecholamines from the high affinity site of tyrosine hydroxylase, phosphorylation of Ser31 induces a small (1.2-2fold) increase in tyrosine hydroxylase activity in vitro primarily by decreasing the KM for the cosubstrate tetrahydrobiopterin, prior phosphorylation of Ser19 or Ser31 is able to increase the rate of phosphorylation of Ser40 by approximately 3fold and 9fold, respectively. Isoform TH1 is phosphorylated at Ser31 in vitro by extracellular signal-regulated protein kinase, while isoform TH2 cannot be phosphorylated at the equivalent Ser31 residue (Ser35) by extracellular signalregulated protein kinase.
phosphoprotein
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Ser31 and Ser40 are readily phosphorylated to activate tyrosine hydroxylase type 1 in vitro. Although phosphorylation of Ser19 does not directly activate tyrosine hydroxylase, chaperone 14-3-3 protein binds and activates tyrosine hydroxylase at Ser19 phosphorylated by Ca2+/calmodulin-dependent protein kinase II.
phosphoprotein
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the enzyme is phosphorylated at Ser40 by cAMP-dependent protein kinase
phosphoprotein
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phosphorylation at N-terminal of the enzyme can activate its activity
phosphoprotein
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phosphorylation at the Ser-31 site may regulate enzyme subcellular localization by enabling its transport along microtubules and is necessary for enzyme association with vesicles
phosphoprotein
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the enzyme is phosphorylated by cAMP-dependent protein kinases at serine residues, e.g. Ser31
phosphoprotein
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cyclin-dependent kinase 5 phosphorylates tyrosine hydroxylase, but does not induce the enzyme expression
phosphoprotein
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reversible phosphorylation at Ser40 regulates the enzyme activity, the phosphorylated enzyme is active, dephosphorylation is performed by phosphatase PP2A, PKCdelta physically associates with the PP2A catalytic subunit and phosphorylates the phosphatase to increase its activity, it also physically associates with tyrosine hydroxylase, inhibition of PKCdelta reduces the dephosphorylation activity of PP2A and thereby increases TH-Ser40 phosphorylation, tyrosine hydroxylase activity, and dopamine synthesis, overview
phosphoprotein
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short term regulation of tyrosine hydroxylase depends on the phosphorylation of seryl residues, Ser19, Ser31, and Ser40, in the TH regulatory domain, activating phosphorylation at Ser40 is inhibited by alpha-synuclein
phosphoprotein
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phosphorylation occurs at S8, S19, S31 and S40. Neither cAMP-dependent protein kinase nor extracellular signal-regulated kinase 2 activity for phosphorylation of tyrosine hydroxylase is affected by pre-existing phosphorylations. Phosphorylation of S40 by cAMP-dependent protein kinase is inhibited by bound dopamine
phosphoprotein
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AMP-activated protein kinase activates the enzyme by reversible phosphorylation at Ser19, Ser31, and Ser40, activated by 5-aminoimidazole-4-carboxamide-1-beta-4-ribofuranoside and inhibited by PD-098059, compound C and 5'-amino-5'-dAdo, PD-098059 specifically inhibits phosphorylation at Ser31 without affecting phosphorylation at Ser19 and Ser40
phosphoprotein
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phosphorylation of Ser40 activtes the enzyme by reversing the inhibition by dopamine binding
phosphoprotein
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reversible phosphorylation at Ser40 is required for enzyme activation, inhibited by the nociceptin/orphanin FQ-NOP receptor system, while phosphorylation on Ser31 is unaffected
phosphoprotein
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the enzyme is phosphorylated at Ser19, Ser31, and Ser40, leading to its activation
phosphoprotein
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the enzyme is regulated by phosphorylation of Ser19, Ser31, and Ser40, overview
phosphoprotein
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enzyme molecules phosphorylated at their Ser31 and Ser40 are localized predominantly in the cytoplasm of PC12D cells. However, those molecules phosphorylated at Ser19 are found mainly in the nucleus, whereas they are negligible in the cytoplasm. The phosphorylation of the N-terminal portion regulates the degradation of this enzyme by the ubiquitin-proteasome pathway
phosphoprotein
phosphorylation at the Ser-31 site may regulate enzyme subcellular localization by enabling its transport along microtubules and is necessary for enzyme association with vesicles
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nitration at N-terminal of the enzyme can inactivate its activity
additional information
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S-glutathionylation at N-terminal of the enzyme can inactivate its activity