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Information on EC 1.14.17.1 - dopamine beta-monooxygenase
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EC Tree
1.14.17.1 dopamine beta-monooxygenaseIUBMB Comments
A copper protein. The enzyme, found in animals, binds two copper ions with distinct roles during catalysis. Stimulated by fumarate.
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Word Map
- 1.14.17.1
- catecholamine
-
noradrenergic
- norepinephrine
- nerve
-
sympathetic
- noradrenaline
- adrenal
-
innervation
- medulla
- fiber
-
dopaminergic
-
neuropeptide
-
chromaffin
-
adrenergic
-
monoamine
-
neurotransmitter
- ganglia
- coeruleus
- hypothalamus
-
catecholaminergic
- phenylethanolamine
- npy
- epinephrine
-
cholinergic
- adrenaline
-
phenylethanolamine-n-methyltransferase
- n-methyltransferase
-
varicosity
-
vasoactive
-
rostrally
- reserpine
-
gene-related
-
catecholamine-synthesizing
- disulfiram
- peptidylglycine
-
preganglionic
-
adrenomedullary
-
th-immunoreactive
-
orthostatic
-
preoptic
-
ventrolateral
-
monoaminergic
-
parabrachial
- saporin
-
intermediolateral
-
hydroxylase-immunoreactive
-
cytoarchitectonic
- medicine
- drug development
- postrema
- diagnostics
-
histofluorescence
- alpha-methyl-p-tyrosine
The enzyme appears in viruses and cellular organisms
Synonyms
dopamine-beta-hydroxylase, dopamine beta-hydroxylase, dbetah, dopamine beta hydroxylase, dopamine beta-monooxygenase, dopamine-beta-monooxygenase, plasma dopamine beta-hydroxylase, dbetam, dopamine-b-hydroxylase, plasma dbetah activity, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3,4-dihydroxy-phenylethylamine, ascorbate: oxygen oxidoreductase (3-hydroxylating)
-
-
3,4-dihydroxyphenethylamine beta-oxidase
-
-
-
-
3,4-dihydroxyphenylethylamine beta-hydoxylase
-
-
-
-
4-(2-aminoethyl)pyrocatechol beta-oxidase
-
-
-
-
DbetaH
DBH
DBM
Dopa beta-hydroxylase
-
-
-
-
dopamine beta-hydrolase
-
-
-
-
dopamine beta-hydroxylase
dopamine beta-mono-oxygenase
dopamine beta-oxidase
-
-
-
-
dopamine hydroxylase
-
-
-
-
dopamine(3,4-dihydroxyphenethylamine)beta-mono-oxygenase
-
-
-
-
dopamine-beta-hydroxylase
EC 1.14.2.1
-
-
formerly
-
oxygenase, dopamine beta-mono-
-
-
-
-
phenylamine beta-hydroxylase
-
-
-
-
dopamine beta-hydroxylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O
-
-
-
-
dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O
mechanism
-
dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O
stoichiometry
-
dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O
ping pong mechanism
-
dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O
uni-uni bi-uni ping pong mechanism
-
dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O
new mechanism of enzyme
-
dopamine + 2 ascorbate + O2 = noradrenaline + 2 monodehydroascorbate + H2O
during the reaction, an O atom from molecular O2 is inserted at the beta-carbon in dopamine with retention of configuration, and the second O atom goes to water. The reaction also requires two electrons provided by two ascorbate molecules that are oxidized to semihydroascorbate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
dopamine,ascorbate:oxygen oxidoreductase (beta-hydroxylating)
A copper protein. The enzyme, found in animals, binds two copper ions with distinct roles during catalysis. Stimulated by fumarate.
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CAS REGISTRY NUMBER
COMMENTARY
9013-38-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(4-hydroxybenzyl)imidazole + ascorbate + O2
4-hydroxybenzaldehyde + dehydroascorbate + H2O + ?
-
-
-
?
1-phenyl-1-aminomethylethene + ascorbate + O2
2,3-dihydroxy-2-phenylpropylamine + dehydroascorbate + H2O + ?
-
ascorbate and ferrocyanide can function as a electron donors
-
?
2-aminoindane + ascorbate + O2
trans-(1S,2S)-2-amino-1-indanol + H2O
-
Stereochemistry is in contrast to the stereochemical course of pro-R hydroxylation of the DBH/phenethylamine reaction. Studies with stereospecifically deuterium labelled substrate show that the production of (1S)-aminoindanol ir the result of sterospecific pro-S hydrogen abstraction followed by the oxygen binding with overall retention of configuration
-
?
2-bromo-3-(p-hydroxyphenyl)-1-propene + ascorbate + O2
2-bromo-3-hydroxy-3-(p-hydroxyphenyl)-1-propene + H2O
-
-
-
?
2-chlorophenethylamine + ascorbate + O2
2-amino-1-chloro-1-phenylethanol + dehydroascorbate + H2O
-
-
-
?
2-hydroxyphenethylamine + ascorbate + O2
2-amino-1-phenylethane-1,1-diol + dehydroascorbate + H2O
-
-
-
?
4-hydroxybenzyl cyanide + ascorbate + O2
4-hydroxymandelonitrile + dehydroascorbate + H2O
-
and benzyl cyanide analogs
-
?
4-hydroxyphenyl-2-aminoethyl sulfide + ascorbate + O2
4-hydroxyphenyl-2-aminoethyl sulfoxide + dehydroascorbate + H2O
-
-
-
?
4-hydroxyphenyl-2-aminopropyl selenide + ascorbate + O2
4-hydroxyphenyl-2-aminopropyl selenoxide + dehydroascorbate + H2O
-
-
-
?
beta,beta-dideuterated tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
-
-
-
-
?
dopamine + ascorbate + O2
norepinephrine + dehydroascorbate + H2O
-
-
-
-
?
phenyl 2-aminoethyl sulfide + ascorbate + O2
phenyl-2-aminoethyl sulfoxide + dehydroascorbate + H2O
tyramine + ascorbate + N,N,N',N'-tetramethyl-p-phenylenediamine
octopamine + dehydroascorbate + ?
-
-
-
-
?
tyramine + ascorbate + N,N-dimethyl-p-phenylenediamine
octopamine + dehydroascorbate + ?
-
-
-
-
?
tyramine + N-(4-chlorophenyl)-N'-hydroxyguanidine + O2
octopamine + 1-(4-chlorophenyl)urea + (4-chlorophenyl)cyanamide + 1-oxo-2-(4-chlorophenyl)guanidine + H2O
-
-
-
-
?
tyramine + N-(4-isopropylphenyl)-N'-hydroxyguanidine + O2
octopamine + 1-(4-isopropylphenyl)urea + (4-isopropylphenyl)cyanamide + 1-oxo-2-(4-isopropylphenyl)guanidine + H2O
-
33% of the activity with N-(4-methoxyphenyl)-N-hydroxyguanidine
-
-
?
tyramine + N-(4-methoxyphenyl)-N'-hydroxyguanidine + O2
octopamine + 1-(4-methoxyphenyl)urea + (4-methoxyphenyl)cyanamide + 1-oxo-2-(4-methoxyphenyl)guanidine + H2O
-
-
-
-
?
tyramine + N-(4-methylphenyl)-N'-hydroxyguanidine + O2
octopamine + 1-(4-methylphenyl)urea + (4-methylphenyl)cyanamide + 1-oxo-2-(4-methylphenyl)guanidine + H2O
-
116% of the activity with N-(4-methoxyphenyl)-N-hydroxyguanidine
-
-
?
tyramine + N-(4-trifluoromethylphenyl)-N'-hydroxyguanidine + O2
octopamine + 1-(4-trifluoromethylphenyl)urea + (4-trifluoromethylphenyl)cyanamide + 1-oxo-2-(4-trifluoromethylphenyl)guanidine + H2O
-
16% of the activity with N-(4-methoxyphenyl)-N-hydroxyguanidine
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
N,N-dimethyl-1,4-phenylenediamine and ascorbic acid derivates are efficient reductants for the enzyme
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
ferrocyanide can function as a electron donor
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
D-xyloascorbic acid, L-araboascorbic acid or D-araboascorbic acid can replace L-xyloascorbic acid
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
3,4-dihydroxyphenethylamine is identical with 4-(2-aminoethyl)-1,2-benzendiol i.e. dopamine, ferricyanide can replace ascorbate
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
norepinephrine
?
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
phenyl 2-aminoethyl sulfide + ascorbate + O2
phenyl-2-aminoethyl sulfoxide + dehydroascorbate + H2O
-
-
-
-
?
phenyl 2-aminoethyl sulfide + ascorbate + O2
phenyl-2-aminoethyl sulfoxide + dehydroascorbate + H2O
-
and derivates
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
-
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
-
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
-
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
-
-
-
-
?
additional information
?
-
-
evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase
-
-
?
additional information
?
-
-
the zinc finger transcription factor GATA-3 regulates the transcriptional activity of dopamine beta-hydroxylase, protein-protein interaction analyses both in vitro and in vivo, overview
-
-
?
additional information
?
-
-
the zinc finger transcription factor GATA-3 positively regulates the transcriptional activity of dopamine beta-hydroxylase, protein-protein interaction analyses both in vitro and in vivo, interaction between the two transcription factors GATA-3 and Sp1, overview
-
-
?
additional information
?
-
-
a significantly lower plasma DBH activity is found in combat veterans with posttraumatic stress disorder carrying the CC genotype as compared to veterans without posttraumatic stress disorder carrying the corresponding genotype, dependent on the genotype the regulation of DBH expression is different in response to trauma, overview
-
-
?
additional information
?
-
-
the plasma dopamine beta-hydroxylase activity is correlated with polymorphisms in the DBH gene in Eastern Indian population, overview
-
-
?
additional information
?
-
-
the zinc finger transcription factor GATA-3 regulates the transcriptional activity of dopamine beta-hydroxylase, protein-protein interaction analyses both in vitro and in vivo, overview
-
-
?
additional information
?
-
-
the zinc finger transcription factor GATA-3 positively regulates the transcriptional activity of dopamine beta-hydroxylase, protein-protein interaction analyses both in vitro and in vivo, overview
-
-
?
additional information
?
-
-
a noradrenalin-synthesizing enzyme from dopamine
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dopamine + ascorbate + O2
norepinephrine + dehydroascorbate + H2O
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
-
?
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
-
-
-
?
additional information
?
-
-
the zinc finger transcription factor GATA-3 regulates the transcriptional activity of dopamine beta-hydroxylase, protein-protein interaction analyses both in vitro and in vivo, overview
-
-
?
additional information
?
-
-
a significantly lower plasma DBH activity is found in combat veterans with posttraumatic stress disorder carrying the CC genotype as compared to veterans without posttraumatic stress disorder carrying the corresponding genotype, dependent on the genotype the regulation of DBH expression is different in response to trauma, overview
-
-
?
additional information
?
-
-
the plasma dopamine beta-hydroxylase activity is correlated with polymorphisms in the DBH gene in Eastern Indian population, overview
-
-
?
additional information
?
-
-
the zinc finger transcription factor GATA-3 regulates the transcriptional activity of dopamine beta-hydroxylase, protein-protein interaction analyses both in vitro and in vivo, overview
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
DBH is an ascorbate-dependent glycoprotein that requires two type 2 bound copper ions per subunit to be active
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
Mg2+
-
regulates the translation of enzyme and affects the ratio of the two glycosylated forms of the enzyme
additional information
Cu2+
-
2,6-dimethylphenyl isocyanide as the isocyanide ligand demonstrated, first: the formation of a mono-DIMPI-four-coordinate complex at each copper, second: the formation of complexes containing more than one isocyanide per copper
Cu2+
-
1.1 Cu2+/subunit, increasing stimulation of activity by addition of up to 1 Cu2+/subunit, further additions up to at least 4 Cu/subunit gave neither stimulation nor inhibition
Cu2+
-
enzyme contains a constant amount of Cu2+, 2 mol per mol of protein, and a variable amount of Cu2+, copper content is a linear function of the purity of the enzyme
Cu2+
-
tyramine can bind to either the Cu(I) or Cu(II) forms of TbetaM
Cu2+
-
enzyme not activated by exogenous copper but activity decreases at high concentrations
Cu2+
-
The enzyme contains two copper centers, one performs the substrate hydroxylation, while the second is used for electron storage/transfer
Cu2+
DBH is an ascorbate-dependent glycoprotein that requires two type 2 bound copper ions per subunit to be active. copper sites are labile and termed CuH and CuM, respectively. CuH is coordinated to three histidines and CuM to two histidines and a methionine. CuM is involved in dioxygen binding and is the site for substrate hydroxylation, and CuH is the site of electron transfer
Cu2+
-
enzyme not activated by exogenous copper but activity decreases at high concentrations
additional information
the structure of the common DOMON (dopamine beta-monooxygenase N-terminal) domain reveals a possible metal-binding site and a ligand-binding pocket, coordinating residues are Asp99, Leu100, Ala115, and Asp130
additional information
-
Cu2+, Mn2+, Ni2+, Co2+, Zn2+, Pb2+, Fe2+, Fe3+ reduce translation of enzyme at concentrations above 1.5 mM, Ni2+ and Cu2+ inhibit the glycosylation
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
tyramine
-
rate of ascorbate reduction of the E-Cu(II) form of TbetaM is also reduced at high tyramine
ascorbate
-
very strong substrate inhibition that is dependent on the level of the co-substrate, O2, and reductant as well as substrate deuteration, substrate inhibition ameliorated at very high ascorbate levels
additional information
-
ascorbic acid derivates inhibit the enzyme at higher concentrations
-
additional information
-
dithiocarbamate pesticides: increase of inhibitory potency from methyl- and dimethyldithiocarbamates to diethyldithiocarbamates up to the most potent ethylenbisdithiocarbamates
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbic acid
-
complete dependance on added ascorbate, e.g. isoascorbate, glucoascorbate, D-ascorbate
Cl-
-
the enzyme is inactive inactive in absence of activating anion at pH 5.1-5.3, high catalytic activity in presence of 0.05-0.6 M Cl- in 50 mM Mes buffer. 0.6 M Cl- increases the optimum concentration of ferrocyanide from 0.25 mM to 2 mM
cytochrome b561
-
in ascorbate-loaded vesicle membranes can supply electron equivalents to support extravesicular dopamine beta-hydroxylase activity without the addition of any mediator, this activity is enhanced significantly by the addition of ferricyanide
-
ferricyanide
-
in ascorbate-loaded vesicle membranes can supply electron equivalents to support extravesicular dopamine beta-hydroxylase activity without the addition of any mediator, this activity is enhanced significantly by the addition of ferricyanide
phosphate
-
the enzyme is inactive inactive in absence of activating anion at pH 5.1-5.3, high catalytic activity in presence of 0.1 M phosphate buffer
acetate
-
the enzyme is inactive inactive in absence of activating anion at pH 5.1-5.3, high catalytic activity in presence of 0.2 M acetate buffer
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.8
2-aminoindane
-
37°C, 0.2 M acetate buffe, pI 6, with 30 mM NEM, 1 mM K4Fe(CN)6, 5 mM CuSO4
0.0906
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.907 mM O2, pH 6 and 35°C
0.145
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.395 mM O2, pH 6 and 35°C
0.177
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.119 mM O2, pH 6 and 35°C
0.178
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.215 mM O2, pH 6 and 35°C
0.193
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 1.039 mM O2, pH 6 and 35°C
0.203
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.587 mM O2, pH 6 and 35°C
0.231
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.056 mM O2, pH 6 and 35°C
0.233
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.907 mM O2, pH 6 and 35°C
0.245
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.214 mM O2, pH 6 and 35°C
0.257
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.110 mM O2, pH 6 and 35°C
0.316
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.598 mM O2, pH 6 and 35°C
0.328
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.416 mM O2, pH 6 and 35°C
0.341
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.063 mM O2, pH 6 and 35°C
0.5 - 2
tyramine
-
enzyme from serum of 5-weeks-old rats, at 37°C, pH not specified in the publication
0.79
tyramine
-
enzyme from serum of 2-weeks-old rats, at 37°C, pH not specified in the publication
0.92
tyramine
-
enzyme from serum of 8-weeks-old rats, at 37°C, pH not specified in the publication
1.22
tyramine
-
enzyme from serum of 1-weeks-old rats, at 37°C, pH not specified in the publication
1.37
tyramine
-
enzyme from serum of 12-weeks-old rats, at 37°C, pH not specified in the publication
1.6
tyramine
-
enzyme from serum of 15-weeks-old rats, at 37°C, pH not specified in the publication
2.1
tyramine
-
enzyme from serum of 27-weeks-old rats, at 37°C, pH not specified in the publication
additional information
additional information
-
Km of ascorbate, tyramine and O2 as a function of pH and fumarate activation
-
additional information
additional information
-
Km of benzyl cyanide analogs with or without 6% dimethylformamide
-
additional information
additional information
-
comparison of Km of native enzyme and dimeric and tetrameric species after treatment with dithiothreitol and iodoacetamide
-
additional information
additional information
-
Km of N,N-dimethyl-1,4-phenylenediamine and ascorbic acid derivatives
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.95
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 10 mM ascorbate, 0.056 mM O2, pH 6 and 35°C
5.8
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 50 mM ascorbate, 0.063 mM O2, pH 6 and 35°C
9.6
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 50 mM ascorbate, 0.110 mM O2, pH 6 and 35°C
10.9
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 10 mM ascorbate, 0.119 mM O2, pH 6 and 35°C
13.5
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 50 mM ascorbate, 0.214 mM O2, pH 6 and 35°C
14.3
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 10 mM ascorbate, 0.215 mM O2, pH 6 and 35°C
19.4
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 10 mM ascorbate, 0.395 mM O2, pH 6 and 35°C
19.4
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 50 mM ascorbate, 0.416 mM O2, pH 6 and 35°C
20.1
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 10 mM ascorbate, 0.587 mM O2, pH 6 and 35°C
24.6
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 50 mM ascorbate, 0.598 mM O2, pH 6 and 35°C
29.2
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 50 mM ascorbate, 0.907 mM O2, pH 6 and 35°C
38.6
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 50 mM ascorbate, 1.039 mM O2, pH 6 and 35°C
39.4
beta,beta-dideuterated tyramine
Drosophila sp. (in: flies)
-
at 10 mM ascorbate, 0.907 mM O2, pH 6 and 35°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.25
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.587 mM O2, pH 6 and 35°C
2
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.907 mM O2, pH 6 and 35°C
2.1
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.215 mM O2, pH 6 and 35°C
2.4
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.395 mM O2, pH 6 and 35°C
2.8
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.119 mM O2, pH 6 and 35°C
2.8
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.416 mM O2, pH 6 and 35°C
2.86
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 1.039 mM O2, pH 6 and 35°C
3.3
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.598 mM O2, pH 6 and 35°C
3.35
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.056 mM O2, pH 6 and 35°C
4
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.907 mM O2, pH 6 and 35°C
6
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.110 mM O2, pH 6 and 35°C
7.4
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.063 mM O2, pH 6 and 35°C
7.8
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.214 mM O2, pH 6 and 35°C
additional information
additional information
-
KI as function of pH and fumarate activation
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme activity in plasma from combat veterans with or without chronic posttraumatic stress disorder, overview
additional information
-
activity in the cat is twofold higher compared to rat
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
without anion activation or reaction with N,N,N,N-tetramethyl-p-phenylenediamine activated with 0.6 M Cl-
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6.5
-
sharp decrease in activity between pH 4.5 and 5.0 and between pH 6.0 and 6.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
438589, 438597, 438599, 438601, 438604, 438606, 438607, 438608, 438609, 438610, 438611, 438612, 438613, 438614, 438615, 438616, 438617, 438618, 438619, 438620, 438621, 438622, 438623, 438624, 438626, 438627, 438628, 438629, 438630, 438634, 438635, 651186, 657766, 657814, 659086, 659287, 659320
-
-
brenda
spontaneously hypertensive rat (SHR) and age-matched Wistar Kyoto rats (WKY/Izm)
UniProt
brenda
-
-
-
brenda
Hsd:ICR (CD-1) outbred albino mice, postnatal day 27 male mice and day 28 male mice
-
-
brenda
-
-
-
brenda
spontaneously hypertensive rat (SHR) and age-matched Wistar Kyoto rats (WKY/Izm)
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
primary culture of trunk region of quail eggs, overview
brenda
-
the DBH activity:DBH protein ratio is the same in human serum and cerebrospinal fluid and does not change in patients with Parkinson disease, whose cerebrospinal fluid has very low DBH activity and protein levels compared with cerebrospinal fluid from healthy individuals
brenda
-
a 75% decrease of dopamine-beta-hydroxyase expression is observed in rats exposed to 2,4-dichlorophenoxyacetic acid through lactation for 14 days
brenda
additional information
-
dietary copper deficiency is associated with increased formation of enzyme
brenda
-
-
438597, 438601, 438604, 438606, 438607, 438613, 438614, 438615, 438617, 438619, 438621, 438623, 438624, 438628, 438629, 438630, 438635, 657766, 657814, 659086
brenda
-
a functional -1021C3T polymorphism in the DBH gene regulates plasma DBH activity, and individuals with the genotype T/T have genetically determined low DBH activity in their plasma
brenda
-
dopamine beta-hydroxyase is reduced in rats subjected to chronic mild stress for 5 weeks. Imipramine treatment minimizes these chronic mild stress-induced reductions
brenda
-
enzyme activity in children and adolescents increases with the age between 3-10 years, later it decreases approximately by the age of 10-14 years. At the age of 21 to 60 years the dopamine-beta-hydroxylase level is stable
brenda
-
activity is highest in 5-day-old rats, it decreases till the age of 14 days and increases mainly in 14-day to 35-day-old animals, significant decrease in activity in rats between 35 to 40 days, adult rats aged 90-120 days show a stable activity of dopamine bet-hydroxylase
brenda
age-related changes in immunoreactivity for dopamine beta-hydroxylase in carotid body glomus cells in spontaneously hypertensive rats
brenda
-
age-related changes in immunoreactivity for dopamine beta-hydroxylase in carotid body glomus cells in spontaneously hypertensive rats
-
brenda
-
axons expressing dopamine beta hydroxyase frequenty made appositions to sympathetic and parasympathetic preganglionic neurons
brenda
-
enzyme activity in plasma from combat veterans with or without chronic posttraumatic stress disorder, non-normal distribution, overview
brenda
-
taste disc of the tongue, DBH-like immunoreactive cells are located in the intermediate layer in the taste disc, the cells show an apical process reaching the surface of the disc and one or several basal processes, overview
brenda
-
DBM protein is present in Cu-negative samples but not in Cu-positive samples
brenda
additional information
gDBH expression is found between the hypothalamus-pituitary and oviduct during the ovulation phase and the broody phase, real-time quantitative PCR enzyme expression analysis. The enzyme expression is higher in animals with higher egg production than in those with low egg production. Analysis of temporal expression patterns of gDBH expression in the hypothalamus, pituitary, ovary, and oviduct tissues during different stages of the goose reproductive cycle, specifically the pre-laying stage, ovulation, oviposition, and the broody phase reveals that the expression is lowest in all tissues during the oviposition phase. It is high in the hypothalamus, ovary, and pituitary in the pre-laying period. High expression of DBH is also found in the cerebrum and cerebellum due to the involvement of norepinephrine and epinephrine in neuroendocrine processes
brenda
additional information
-
immunohistochemic localization analysis, overview
brenda
additional information
determination of tissue distribution of enzyme expression by quantitative real-time PCR enzyme expression analysis
brenda
additional information
-
determination of tissue distribution of enzyme expression by quantitative real-time PCR enzyme expression analysis
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
-
brenda
-
the membranous enzyme may be the physiologically functional form
brenda
additional information
-
enzyme-immunoreactive cells in anterior tuberal nucleus, locus coeruleus and caudal rhombencephalon
-
brenda
additional information
-
enzyme is studied in chromaffin granule ghosts: channeling of dopamine between monoamine transporter and membranous dopamine-beta-monooxygenase
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
DBH is a member of a small unique class of copper-containing hydroxylases that are found in eukaryotes, and all play a critical role in the biosynthesis of neurotransmitters and hormones. The other members of the family are the bifunctional enzyme peptidylglycine alpha-hydroxylating (and alpha-amidating) monooxygenase (PHM), monooxygenase X (DBH-like monooxygenase protein 1, MOXD1), and tyramine beta-monooxygease (TBH), which is the insect homologue of DBH
evolution
the enzyme belongs to the copper type II, ascorbate-dependent monooxygenases
evolution
-
the enzyme belongs to the copper type II, ascorbate-dependent monooxygenases
malfunction
-
dopamine-beta-hydroxylase knockout mice are more sensitive to stress but survive a single 2 h restraint stress in a tube. Disruption of the DBH gene blocks the stress-induced elevation of tyrosine hydroxylase mRNA levels in adrenal medulla but increases phenylethanolamine N-methyltransferase gene expression in both adrenal medulla and stellate ganglia
malfunction
-
in the GRDBHCre mice, glucocorticoid receptor (GR) immunoreactivity is lost in chromaffin cells but is unaltered in the cortex, which leads to the loss of the A-synthesizing enzyme phenylethanolamine-N-methyl-transferase (PNMT). GRDBHCre mutants are viable and fertile and do not appear different from control littermates. Degeneration of the adrenal medulla in young GRDBHCre mutants
malfunction
-
no major role of the -1021C>T polymorphism or the gene itself in the development of cocaine addiction in a Brazilian sample of 689 cocaine addicts and 832 healthy controls, even after correction for sex age, education and population stratification
malfunction
enzyme activity and norepinephrine level in shrimps downregulated by LvDBH-dsRNA are reduced, the treated animals show increased susceptibility to Vibrio alginolyticus infection, significantly lower total hemocyte count, phagocytic activity, clearance efficiency, and resistance to Vibrio alginolyticus infection are observed in shrimp that received LvDBH-dsRNA at 3 days post injection compared to those injected with diethyl pyrocarbonate-water or non-targeting gene-dsRNA
malfunction
enzyme LvDBH inhibited or silenced in haemocytes by disulfiram and LvDBH-dsRNA, repectively, results in impaired synthesis of norepinephrine from dopamine in hemolymph
malfunction
genotype-phenotype correlations. Mutant L317P shows secretory deficiency and is localized in the endoplasmic reticulum
physiological function
-
DBH promoter contains at least one functional Egr1 motif, Egr1 may play a role in the physiological regulation of transcription of the DBH gene
physiological function
-
determinant role of Phox2a and Phox2b on the expression and function of DBH in vitro
physiological function
Drosophila sp. (in: flies)
-
tyramine beta-monooxygenase is homologous to mammalian dopamine beta-monooxygenase, tighter regulation of neurotransmitter levels by the insect enzyme than in the mammalian homologue
physiological function
dopamine beta-hydroxylase (DBH) catalyzes the conversion of dopamine to norepinephrine in the biosynthesis of catecholamines. The enzyme plays a critical role in catecholamine synthesis of neuroendocrine regulatory network, and is suggested to be involved in the immunoendocrine responses of invertebrate against bacterial challenge
physiological function
dopamine beta-hydroxylase (DBH) is a copper-containing monooxygenase enzyme that plays an important role in catecholamine synthesis of the neuroendocrine regulatory network. In shrimp, the biosynthesis of catecholamines, including dopamine and norepinephrine, is required for physiological and immunological responses against stress
physiological function
dopamine beta-hydroxylase (DBH) is the enzyme catalyzing the synthesis of noradrenaline from dopamine, it is stronger in the glomus cells of spontaneously hypertensive SHR/Izm rats than in those of Wistar Kyoto WKY/Izm rats
physiological function
dopamine beta-hydroxylase catalyzes the conversion of dopamine to norepinephrine in the biosynthesis of catecholamines
physiological function
dopamine beta-hydroxylase catalyzes the conversion of dopamine to norepinephrine in the biosynthesis of catecholamines. Effect of wild-type and mutant alpha-SYN on cAMP response element (CRE)-mediated regulation of the norepinephrine-synthesizing enzyme dopamine beta-hydroxylase (DBH): overexpression of wild-type or mutant human alpha-SYN interfers with CRE-mediated regulation of DBH transcription in norepinephrine-producing SK-N-BE(2) cells. Upon entering the nucleus, alpha-SYN interacts with the DBH promoter region encompassing the CRE, which interfered with forskolin-induced CREB binding to the CRE region. Mutant A53T alpha-SYN shows much higher tendency to nuclear translocation and interaction with the DBH promoter region encompassing the CRE than wild-type. CRE-mediated transcriptional regulation of tyrosine hydroxylase and enzyme DBH plays a crucial role in stress response
physiological function
dopamine beta-hydroxylase catalyzes the conversion of dopamine to norepinephrine in the biosynthesis of catecholamines. Effect of wild-type and mutant human alpha-SYN on cAMP response element (CRE)-mediated regulation of the norepinephrine-synthesizing enzyme dopamine beta-hydroxylase (DBH), stress-induced DBH regulation is modulated in the brains of A53T transgenic mice (A53T Tg). Overexpression of wild-type or mutant human alpha-SYN interfers with CRE-mediated regulation of DBH transcription in murine brains of A53T transgenic mice (A53T Tg). Upon entering the nucleus, alpha-SYN interacts with the DBH promoter region encompassing the CRE, which interfers with forskolin-induced CREB binding to the CRE region. Mutant A53T alpha-SYN shows much higher tendency to nuclear translocation and interaction with the DBH promoter region encompassing the CRE than wild-type
physiological function
dopamine beta-hydroxylase is a critical enzyme in the biosynthesis of catecholamines with a role in neuroendocrine regulation and in avian reproduction. Dopamine beta-hydroxylase catalyzes the conversion of dopamine to norepinephrine in the biosynthesis of catecholamines. The activity of DBH influences the levels of dopamine and the biosynthesis of norepinephrine and epinephrine. The enzyme is important in the nervous system
physiological function
dopamine-beta-hydroxylase (DBH) is an oxidoreductase that is primarily responsible for the conversion of dopamine to norepinephrine. DBH is widely regarded as a disease-modifying gene in psychiatric diseases
physiological function
-
dopamine beta-hydroxylase (DBH) is the enzyme catalyzing the synthesis of noradrenaline from dopamine, it is stronger in the glomus cells of spontaneously hypertensive SHR/Izm rats than in those of Wistar Kyoto WKY/Izm rats
-
Show AA Sequence and Transmembrane Helices (654 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
220000 - 250000
-
220000 Da, L208 homoenzyme, 230000 Da, F208 homoenzyme, 250000 Da, F208/L208 heteroenzyme, low-angle laser light scattering-photometry
260000
-
native enzyme, low-angle laser light scattering photometry coupled with high-performance gel filtration
290000
300000
72000
75000
80000
-
4 * 80000, SDS-PAGE after treatment with 2-mercaptoethanol, subunits joined in pairs by disulfide bonds
additional information
-
molecular forms change depending on concentration of salts and kind of salts
290000
-
sedimentation equilibrium analysis, 5 mM potassium phosphate buffer, pH 6.8, 0.1 M NaCl
72000
-
x * 72000, secreted and modified (N-glycosylation) form, Western blot analysis
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer or tetramer
the enzyme occurs borh as dimer and tetramer, which can be separated by size exclusion chromatography. The dimer and tetramer do not interconvert in the pH interval pH 4-9. Under denaturing conditions, the tetramer converts to a dimer, and upon addition of a reducing agent, the dimer converts to a monomer. The dimeric structure is asymmetric. In the A chain, the two catalytic CuH and CuM domains are in a closed conformation, and in the B chain, they adopt the same open conformation as seen in peptidylglycine alpha-hydroxylating (and alpha-amidating) monooxygenase (PHM), the catalytic CuH domain in chain A is moved away from the DOMON domain and closer to the catalytic CuM domain. The DOMON domain has an immunoglobulin (Ig)like beta-sandwich structure, the catalytic core (the CuH and CuM domains) has the same topology as the structure of PHM, and the dimerization domains consisting of two antiparallel alpha helices form a four-helix bundle. Following the dimerization domain, there is a beta-strand (residues 561 to 566) taking part in the catalytic CuM domain and a beta-strand (residues 608 to 614) that is part of the DOMON domain, creating a very integrated structure, coordinating residues are Asp99, Leu100, Ala115, and Asp130. The DOMON domain and the dimerization domain are linked via C154-C596. Chain A is linked via two intermolecular disulfide bonds with chain B in the dimerization domain. Enzyme structure analysis, detailed overview
tetramer
additional information
?
-
x * 72000, secreted and modified (N-glycosylation) form, Western blot analysis
tetramer
-
4 * 66000-74000, SDS-PAGE after cleavage of intersubunit disulfide bonds with dithiothreitol, tetramer consists of two disulfid-linked dimers
tetramer
-
4 * 80000, SDS-PAGE after treatment with 2-mercaptoethanol, subunits joined in pairs by disulfide bonds
additional information
the enzyme contains a DOMON domain, a Cu2_monooxygen domain, and three glycosylation sites
additional information
-
the enzyme contains a DOMON domain, a Cu2_monooxygen domain, and three glycosylation sites
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
phospholipoprotein
-
hypothesis: completely processed enzyme may be anchored to cellular membranes by binding to phosphatidylserine
glycoprotein
-
3.5 residues of glucosamine per subunit, glucosamine is the only hexosamine detected
glycoprotein
DBH is an ascorbate-dependent glycoprotein, glycosylation is observed at all four predicted sites: Asn64, Asn184, Asn344, and Asn566
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L208F
-
a natural variant - three phenotypes of enzyme isolated: 4 * L208-homoenzyme, 4 * F208-homoenzyme and 2 * F208, 2 * L208-heteroenzyme, no significant difference in kinetic properties
A318S
A348E
-
retained inside cell in a premature endoplasmic reticulum form, also naturally occuring mutation
C1021T
-
naturally occuring gene polymorphism, determination of the frequency in combat veterans with or without chronic posttraumatic stress disorder, overview
D100E
-
retained inside cell in a premature endoplasmic reticulum form, also naturally occuring mutation
D331N
-
retained inside cell in a premature endoplasmic reticulum form, also naturally occuring mutation
D460N
site-directed mutagenesis, the mutant shows reduced expression levels compared to the wild-type enzyme, the mutant shows reduced expression levels compared to the wild-type enzyme
G482R
the mutation has subsequent effect on the activity of the enzyme as it is present close to the active site
L317P
R549C
W544S
site-directed mutagenesis, the enzyme shows a marginal decrease in homospecific activity, the mutant shows reduced expression levels compared to the wild-type enzyme
additional information
A318S
site-directed mutagenesis, the enzyme shows a marginal decrease in homospecific activity
L317P
site-directed mutagenesis, the mutant shows secretory deficiency and is localized in the endoplasmic reticulum
R549C
the mutation causes abnormal oligomerization through non-native disulfide bond formation
R549C
site-directed mutagenesis, the enzyme shows a marginal decrease in homospecific activity, the mutant shows partial secretory deficiency and is localized in the endoplasmic reticulum
additional information
-
correlation of plasma dopamine beta-hydroxylase activity with polymorphisms in DBH gene in Eastern Indian population, genotyping, allele frequencies and effects of haplotypes, overview
additional information
-
genotypic and haplotypic associations of the DBH gene with plasma dopamine beta-hydroxylase activity in African Americans, genotyping, relationship between DBH polymorphisms and pDbetaH in samples, overview
additional information
LvDBH expression is silenced in thoracic ganglia, haemocytes and hepatopancreas of shrimp by treatment with LvDBH-dsRNA for 3 days, a decrease of DBH contents in haemocytes accompanied by decreased levels of norepinephrine and dopamine in hemolymph are observed
additional information
-
LvDBH expression is silenced in thoracic ganglia, haemocytes and hepatopancreas of shrimp by treatment with LvDBH-dsRNA for 3 days, a decrease of DBH contents in haemocytes accompanied by decreased levels of norepinephrine and dopamine in hemolymph are observed
additional information
-
construction of chimera: dopamine-betamonooxygenase signal, residue 1-42 appended to peptidylglycine alpha-hydroxylating monoxygenase, result: the signal/anchor domain of enzyme is responsible for its membrane association and is likely to play a key role in the targeting of enzyme to secretory garnules in chromaffin cells and adrenergic neurons
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by anion exchange and His tag affinity chromatography, and gel filtration
-
partially, from adrenal medulla after crude extract PEG 6000 precipitation and DEAE-Sepharose chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
C12 cells transfected with expression vector for full length or truncated inactive Egr1 and DBH promoter-driven luciferase constructs p5'DBH/Luc (-1625/+21), p5'DBH/Luc (-247/+21) and p5'DBH/Luc (-200/+21)
-
expression in AtT-20 corticotrope tumor cells, PC12 pheochromocytoma cells and Chinese hamster ovary cells
-
gene DBH containing 12 exons that span approximately 23 kb of human chromosome 9, DNA and amino acid sequence determination and analysis, genotyping of ns/del, rs1611115, rs2519152, and rs6271
-
gene DBH, DNA and amino acid sequence determination and analysis, a GATA-3 response sequence of the distal DBH promoter, the ubiquitously expressed AP4 protein physically interacts with the upstream DBH promoter subdomain at -863 to -858 bp and regulates DBH promoter function, interaction analysis, the AP4 protein-DBH/AP4 DNA complex is not affected by addition of nonspecific Sp1 sequences, overview
-
gene DBH, DNA and amino acid sequence determination and analysis, expression of the GST-tagged enzyme in Escherichia coli strain BL21 (DE3)
-
gene DBH, DNA and amino acid sequence determination and analysis, genotyping, overview
-
gene dbh, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis and tree, quantitative real-time PCR enzyme expression analysis
gene dbh, recombinant expression of wild-type and mutant enzymes in HEK293 cells, generation of transient and stable lines expressing the mutant variant enzymes, genotype-phenotype correlations
gene gDBH, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time quantitative PCR enzyme expression analysis
mouse strain carrying the conditional allele of glucocorticoid receptor (GR) crossed with a transgenic mouse line expressing the Cre recombinase under the control of the DBH gene
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
A53T Tg mice that express human A53T variant alpha-synuclein under the direction of the mouse prion protein promoter show decreased DBH expression. A53T Tg mice exhibit anxiety-like behaviors and abnormal adaptive responses following the repeated immobilization stress
alpha-SYN enters the nucleus and binds directly to the DBH promoter region. alpha-Syn atteniúates the forskolin-induced DBH upregulation in SK-N-BE(2) cells
both in adrenal medulla and stellate ganglia, single immobilization significantly increases DBH mRNA and protein levels both in wild-type and corticotropin-releasing hormone knockout mice
-
Cu-negative samples have significantly higher DBM activity than Cu-positive samples in both adrenal glands (2.4fold) and medulla oblongata/pons (0.9fold), but not vas deferens. No correlation between higher DBM mRNA and lower noradrenaline in Cu-negative tissues
-
DBM protein abundance in adrenal glands is higher in the Cu-negative samples compared with Cu-positive samples
-
Egr1 reduces DBH promoter activity, reduction occurrs as early as 4 h and reaches maximal inhibition 16-40 h after transfection. Egr1 also reduces the expression of endogenous DBH mRNA and the induction of DBH promoter activity by cAMP. The first 247, but not 200, nucleotides of DBH promoter are sufficient for suppression
-
forced expression of Trim11 with Phox2b specifically increases mRNA levels of dopamine beta-hydroxylase gene in primary avian neural crest stem cell culture compared to cultures where only Phox2b is forced expressed
-
forskolin, dexamethasone, ionomycin, and 17-beta-estradiol all induce a significant increase in DBH promoter activity, the most significant 15.8fold upregulation of DBH transcription is observed in forskolin-treated cells The forskolin-induced DBH upregulation in SK-N-BE(2) cells is attenuated by alpha-Syn. CRE-mediated transcriptional regulation of tyrosine hydroxylase and enzyme DBH plays a crucial role in stress response
LvDBH expression is silenced in thoracic ganglia, haemocytes and hepatopancreas of shrimp by treatment with LvDBH-dsRNA for 3 days, a decrease of DBH contents in haemocytes accompanied by decreased levels of norepinephrine and dopamine in hemolymph are observed. LvDBH expressions in thoracic ganglia, haemocytes, and hepatopancreas of shrimp transferred from 28°C to 20°C for 30 min are significant higher than those held at 28°C, hypothermal stress reduces the expression of LvDBH
transfection of 0.1 to 5 microg of cDNAs of Phox2a or Phox2b significantly increases mRNA and protein levels of DBH (up to 47%) in a concentration-dependent manner. Simultanoeus transfection with both Phox2a and Phox2b does not further increase mRNA and protein levels of DBH
-
transfection of shRNAs specific to Phox2a or Phox2b genes significantly reduces mRNA and protein levels of DBH after shutdown of endogenous Phox2, which is accompanied by a decreased [(3)H]norepinephrine uptake. Reduced DBH expression caused by the shRNA specific to Phox2a can be reversed by transfection with Phox2b cDNA and vice versa. Cotransfection with both shRNAs specific to Phox2a and Phox2b genes does not further reduce mRNA and protein levels of DBH
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
genotype-controlled measurement of plasma DBH activity might be used as a potential biological marker of the response to trauma
drug development
inhibitors of enzyme DBH nepicastat and etamicastat are currently in clinical development for treatment of cocaine dependence
medicine
medicine
-
ethanol causes concentration- and time-dependent increase in DBH gene transcription. Protein kinase A, mitogen-activated protein kinase/extracellular signal -regulated kinase kinase, and casein kinase II inhibitors block induction of dopamine beta-hydroxylase and a large subset of ethanol-responsive genes. Ethanol regulation of dopamine beta-hydroxylase requires a functional cAMP-response element and its binding protein and may require interaction of multiple kinase pathways. These studies may have implications for behavioral responses to ethanol or mechanisms underlying ethanol-related neurological disease
medicine
-
the antidepressant drug imipramine counteracts the chronic mild stress-induced reduction of plasma dopamine beta-hydroxylase activity
medicine
-
a -1021C/T polymorphism in human dopamine-beta-hydroxyase shows an correlation with fasting plasma glucose in association with hypertension. CC homozygotes show a steeper increase in probability of hypertension with FPG than T allele carriers
medicine
-
adequate dietary Cu is essential to support DBM function in vivo
medicine
-
simple photometric method in clinical chemistry for determining the DBH activity in human blood, which parallels the protein level, and the high interest in DBH activity in the blood in various diseases that affect central and peripheral catecholamine systems, such as DBH deficiency and pheochromocytoma
medicine
inhibitors of enzyme DBH nepicastat and etamicastat are currently in clinical development for treatment of cocaine dependence
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Merkler, D.J.; Kulathila, R.; Francisco, W.A.; Ash, D.E.; Bell, J.
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Bos taurus
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211
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1981
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Okuno, S.; Fujisawa, H.
Purification and characterization of rat dopamine beta-monooxygenase and monoclonal antibodies to the enzyme
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1984
Rattus norvegicus
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Tian, G.; Berry, J.A.; Klinman, J.P.
Oxygen-18 kinetic isotope effects in the dopamine beta-monooxygenase reaction: Evidence for a new chemical mechanism in non-heme, metallomonooxygenase
Biochemistry
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1994
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Fong, J.C.; Shenkman, L.; Goldstein, M.
Purification and characterization of rat pheochromocytoma dopamine beta-hydroxylase
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1980
Rattus norvegicus
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Colombo, G.; Papadopoulos, N.J.; Ash, D.E.; Villafranca, J.J.
Characterization of highly purified dopamine beta-hydroxylase
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252
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1987
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Human plasma dopamine beta-hydroxylase. Purification and properties
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1978
Homo sapiens
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Purification and characterization of avian dopamine beta-hydroxylase
Biochemistry
20
7423-7431
1981
Gallus gallus
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Aunis, D.; Miras-Portugal, M.T.; Mandel, P.
Bovine adrenal medullary dopamine beta-hydroxylase: purification by affinity chromatography, kinetic studies and presence of essential histidyl residues
Biochim. Biophys. Acta
327
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Bos taurus
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Friedman, S.; Kaufman, S.
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Inhibition of dopamine-beta-hydroxylase by alternative electron donors
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613
62-72
1980
Bos taurus
brenda
May, S.W.; Mueller, P.W.; Padgette, S.R.; Herman, H.H.; Phillips, R.S.
Dopamine-beta-hydroxylase: suicide inhibition by the novel olefinic substrate, 1-phenyl-1-aminomethylethene
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110
161-168
1983
Bos taurus
brenda
Blackburn, N.J.; Collison, D.; Sutton, J.; Mabbs, F.E.
Kinetic and E.P.R. studies of cyanide and azide binding to the copper sites of dopamine (3,4-dihydroxyphenethylamine) beta-mono-oxygenase
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220
447-454
1984
Bos taurus
brenda
Townes, S.; Titone, C.; Rosenberg, R.C.
Inhibition of dopamine beta-hydroxylase by bidentate chelating agents
Biochim. Biophys. Acta
1037
240-247
1990
Bos taurus
brenda
DeWolf, W.E.; Chambers, P.A.; Southan, C.; Saunders, D.; Kruse, L.I.
Inactivation of dopamine beta-hydroxylase by beta-ethynyltyramine: kinetic characterization and covalent modification of an active site peptide
Biochemistry
28
3833-3842
1989
Bos taurus
brenda
DeWolf, W.E.; Carr, S.A.; Varrichio, A.; Goodhart, P.J.; Mentzer, M.A.; Roberts, G.D.; Southan, C.; Dolle, R.E.; Kruse, L.I.
Inactivation of dopamine beta-hydroxylase by p-cresol: isolation and characterization of covalently modified active site peptides
Biochemistry
27
9093-9101
1988
Bos taurus
brenda
Kruse, L.I.; DeWolf, W.E.; Chambers, P.A.; Goodhart, P.J.
Design and kinetic characterization of multisubstrate inhibitors of dopamine beta-hydroxylase
Biochemistry
25
7271-7278
1986
Bos taurus
brenda
Sirimanne, S.R.; Herman, H.H.; May, S.W.
Interaction of dopamine beta-mono-oxygenase with substituted imidazoles and pyrazoles. Catalysis and inhibition
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242
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Bos taurus
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Mechanism-based inhibition of dopamine beta-monooxygenase by aldehydes and amides
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261
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1986
Bos taurus
brenda
Colombo, G.; Rajashekhar, B.; Giedroc, D.P.; Villafranca, J.J.
Alternate substrates of dopamine beta-hydroxylase. I. Kinetic investigations of benzyl cyanides as substrates and inhibitors
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259
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1984
Bos taurus
brenda
Colombo, G.; Rajashekhar, B.; Giedroc, D.P.; Villafranca, J.J.
Mechanism-based inhibitors of dopamine beta-hydroxylase: inhibition by 2-bromo-3-(p-hydroxyphenyl)-1-propene
Biochemistry
23
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1984
Bos taurus
brenda
Klinman, J.P.; Krueger, M.
Dopamine beta-hydroxylase: activity and inhibition in the presence of beta-substituted phenethylamines
Biochemistry
21
67-75
1982
Bos taurus
brenda
May, S.W.; Young, F.K.; Powers, J.L.; Gill-Woznichak, M.M.
Mechanism-based inactivation of dopamine beta-monooxygenase in adrenal chromaffin cells
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228
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Bos taurus
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Izumi, H.; Hayakari, M.; Kondo, Y.; Takemoto, T.
Inhibition of dopamine beta-monooxygenase by histidine
Hoppe-Seyler's Z. Physiol. Chem.
356
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Bos taurus
brenda
Ljones, T.; Skotland, T.; Flatmark, T.
Purification and characterization of dopamine beta-hydroxylase from bovine adrenal medulla
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61
525-533
1976
Bos taurus
brenda
Skotland, T.; Ljones, T.
The enzyme-bound copper of dopamine beta-monooxygenase. Reaction with copper chelators, preparation of the apoprotein, and kinetics of the reconstitution by added copper
Eur. J. Biochem.
94
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1979
Bos taurus
brenda
Adrio, F.; Anadon, R.; Rodriguez-Moldes, I.
Distribution of tyrosine hydroxylase (TH) and dopamine beta-hydroxylase (DBH) immunoreactivity in the central nervous system of two chondrostean fishes (Acipenser baeri and Huso huso)
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448
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2002
Acipenser baerii baerii
brenda
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Reduction of dopamine beta-monooxygenase. A unified model for apparent negative cooperativity and fumarate activation
J. Biol. Chem.
271
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1996
Bos taurus
brenda
Gibson, K.R.; Vanek, P.G.; Kaloss, W.D.; Collier, G.B.; Connaughton, J.F.; Angelichio, M.; Livi, G.P.; Fleming, P.J.
Expression of dopamine beta-hydroxylase in Drosophila Schneider 2 cells. Evidence for a mechanism of membrane binding other than uncleaved signal peptide
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268
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Abudu, N.; Banjaw, M.Y.; Ljones, T.
Kinetic studies on the activation of dopamine beta-monooxygenase by copper and vanadium ions
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257
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Bos taurus
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Selective cleavage and modification of the intersubunit disulfide bonds of bovine dopamine beta-monooxygenase: conversion of tetramer to active dimer
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120
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Bos taurus
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Suzuki, E.; Kurata, T.; Shiabata, M.; Mori, M.; Arakawa, N.
Activities of D- and L-xyloascorbic acid and D- and L-araboascorbic acid as a cofactor for dopamine b-hydroxylase reaction
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43
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Bos taurus
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Effects of disulfiram on serum dopamine-beta-hydroxylase and blood carbon disulphide concentrations in alcoholics
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14
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Homo sapiens
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De Paris, P.; Caroldi, S.
In vitro effect of dithiocarbamate pesticides and of CaNa2EDTA on human serum dopamine-beta-hydroxylase
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8
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Homo sapiens
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Comparative study of biochemical parameters and kinetic properties of dopamine-beta-hydroxylase activity from cat and rat adrenals
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104
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Felis catus, Rattus norvegicus
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Narita, M.; Ishida, T.; Tomoyoshi, T.; Nozaki, M.; Horiike, K.
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396
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Bos taurus
brenda
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Bos taurus
-
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Rattus norvegicus
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Regulation of the translation and processing of rat dopamine beta-hydroxylase by metal ions in a cell free system
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36
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Rattus norvegicus
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Oyarce, A.M.; Steveson, T.C.; Jin, L.; Eipper, B.A.
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Rattus norvegicus
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Bos taurus
-
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Slama, P.; Boucher, J.L.; Reglier, M.
Aromatic N-hydroxyguanidines as new reduction cosubstrates for dopamine beta-hydroxylase
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316
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Bos taurus
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Terland, O.; Flatmark, T.
Anion- and pH-dependent activation of the soluble form of dopamine beta-hydroxylase
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369
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Bos taurus
brenda
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Reversely-oriented cytochrome b561 in reconstituted vesicles catalyzes transmembrane electron transfer and supports extravesicular dopamine beta-hydroxylase activity
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Bos taurus
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Homo sapiens
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Bos taurus
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Wimalasena, D.S.; Wimalasena, K.
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Bos taurus
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Paclt, I.; Koudelova, J.
Changes of dopamine-beta-hydroxylase activity during ontogenesis in healthy subjects and in an experimental model (rats)
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53
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Homo sapiens, Rattus norvegicus
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Grabowska, M.; Schlegel-Zawadzka, M.; Papp, M.; Nowak, G.
Effect of imipramine treatment on plasma dopamine beta-hydroxylase activity in chronic mild stress in rats
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56
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Rattus norvegicus
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Dopamine-beta-hydroxylase immunohistochemical study in the locus coeruleus of neonate rats exposed to 2,4-dichlorophenoxyacetic acid through mothers milk
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29
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Rattus norvegicus
brenda
Abe, M.; Wu, Z.; Yamamoto, M.; Jin, J.J.; Tabara, Y.; Mogi, M.; Kohara, K.; Miki, T.; Nakura, J.
Association of dopamine beta-hydroxylase polymorphism with hypertension through interaction with fasting plasma glucose in Japanese
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28
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Homo sapiens
brenda
Klinman, J.P.
The copper-enzyme family of dopamine b-monooxygenase and peptidylglycine a-hydroxylating monooxygenase: Resolving the chemical pathway for substrate hydroxylation
J. Biol. Chem.
281
3013-3016
2006
Homo sapiens
brenda
Grabowska, M.; Przyslawski, J.; Boleslawska, I.; Schlegel-Zawadzka, M.
Status of serum copper and dopamine beta-hydroxylase (DBH) activity in healthy population
Metal Ions in Biology and Medicine
9
525-529
2006
Rattus norvegicus
-
brenda
Ranson, R.N.; Santer, R.M.; Watson, A.H.
The relationship between serotonin, dopamine beta hydroxylase and GABA immunoreactive inputs and spinal preganglionic neurones projecting to the major pelvic ganglion of Wistar rats
Neuroscience
141
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2006
Rattus norvegicus
brenda
Mustapic, M.; Pivac, N.; Kozaric-Kovacic, D.; Dezeljin, M.; Cubells, J.F.; Mueck-Seler, D.
Dopamine beta-hydroxylase (DBH) activity and -1021C/T polymorphism of DBH gene in combat-related post-traumatic stress disorder
Am. J. Med. Genet. B Neuropsychiatr. Genet.
144B
1087-1089
2007
Homo sapiens
brenda
Bhaduri, N.; Mukhopadhyay, K.
Correlation of plasma dopamine beta-hydroxylase activity with polymorphisms in DBH gene: a study on Eastern Indian population
Cell. Mol. Neurobiol.
28
343-350
2008
Homo sapiens
brenda
Ando, H.; Tomida, M.; Inoue, K.; Asanuma, N.
Dopamine beta-hydroxylase like immunoreactive cells in the frog taste disc
Chem. Senses
32
825-832
2007
Lithobates catesbeianus
brenda
Tang, Y.L.; Epstein, M.P.; Anderson, G.M.; Zabetian, C.P.; Cubells, J.F.
Genotypic and haplotypic associations of the DBH gene with plasma dopamine beta-hydroxylase activity in African Americans
Eur. J. Hum. Genet.
15
878-883
2007
Homo sapiens
brenda
Hong, S.J.; Choi, H.J.; Hong, S.; Huh, Y.; Chae, H.; Kim, K.S.
Transcription factor GATA-3 regulates the transcriptional activity of dopamine beta-hydroxylase by interacting with Sp1 and AP4
Neurochem. Res.
33
1821-1831
2008
Coturnix japonica, Homo sapiens
brenda
Kvetnansky, R.; Krizanova, O.; Tillinger, A.; Sabban, E.L.; Thomas, S.A.; Kubovcakova, L.
Regulation of gene expression of catecholamine biosynthetic enzymes in dopamine-beta-hydroxylase- and CRH-knockout mice exposed to stress
Ann. N. Y. Acad. Sci.
1148
257-268
2008
Mus musculus
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Guindalini, C.; Laranjeira, R.; Collier, D.; Messas, G.; Vallada, H.; Breen, G.
Dopamine-beta hydroxylase polymorphism and cocaine addiction
Behav. Brain Funct.
4
1-4
2008
Homo sapiens
brenda
Hong, S.J.; Chae, H.; Lardaro, T.; Hong, S.; Kim, K.S.
Trim11 increases expression of dopamine beta-hydroxylase gene by interacting with Phox2b
Biochem. Biophys. Res. Commun.
368
650-655
2008
Gallus gallus
brenda
Nelson, K.T.; Prohaska, J.R.
Copper deficiency in rodents alters dopamine beta-mono-oxygenase activity, mRNA and protein level
Br. J. Nutr.
102
18-28
2009
Mus musculus, Rattus norvegicus
brenda
Cheng, S.Y.; Serova, L.I.; Glazkova, D.; Sabban, E.L.
Regulation of rat dopamine beta-hydroxylase gene transcription by early growth response gene 1 (Egr1)
Brain Res.
1193
1-11
2008
Rattus norvegicus
brenda
Nagatsu, T.
Simple photometric assay of dopamine-beta-hydroxylase activity in human blood: Useful in clinical chemistry
Clin. Chem.
55
193-194
2009
Homo sapiens
brenda
Parlato, R.; Otto, C.; Tuckermann, J.; Stotz, S.; Kaden, S.; Groene, H.J.; Unsicker, K.; Schuetz, G.
Conditional inactivation of glucocorticoid receptor gene in dopamine-beta-hydroxylase cells impairs chromaffin cell survival
Endocrinology
150
1775-1781
2009
Mus musculus
brenda
Hess, C.; McGuirl, M.; Klinman, J.
Mechanism of the insect enzyme, tyramine beta-monooxygenase, reveals differences from the mammalian enzyme, dopamine beta-monooxygenase
J. Biol. Chem.
283
3042-3049
2008
Drosophila melanogaster
brenda
Fan, Y.; Huang, J.; Kieran, N.; Zhu, M.Y.
Effects of transcription factors Phox2 on expression of norepinephrine transporter and dopamine beta-hydroxylase in SK-N-BE(2)C cells
J. Neurochem.
110
1502-1513
2009
Homo sapiens
brenda
Zhou, Z.; Wang, L.; Yang, J.; Zhang, H.; Kong, P.; Wang, M.; Qiu, L.; Song, L.
A dopamine beta hydroxylase from Chlamys farreri and its induced mRNA expression in the haemocytes after LPS stimulation
Fish Shellfish Immunol.
30
154-162
2011
Azumapecten farreri (E9JGS5), Azumapecten farreri
brenda
Kim, C.H.; Leung, A.; Huh, Y.H.; Yang, E.; Kim, D.J.; Leblanc, P.; Ryu, H.; Kim, K.; Kim, D.W.; Garland, E.M.; Raj, S.R.; Biaggioni, I.; Robertson, D.; Kim, K.S.
Norepinephrine deficiency is caused by combined abnormal mRNA processing and defective protein trafficking of dopamine beta-hydroxylase
J. Biol. Chem.
286
9196-9204
2011
Homo sapiens
brenda
Rahman, M.K.; Choudhary, M.I.; Islam, M.R.; Hafizur, R.M.
Developmental changes of catecholamine-mediating enzyme - dopamine-beta-hydroxylase and its cofactors in central and peripheral tissues and serum of long-evans rats
Int. J. Biomed. Sci.
8
194-203
2012
Rattus norvegicus
brenda
Kapoor, A.; Shandilya, M.; Kundu, S.
Structural insight of dopamine beta-hydroxylase, a drug target for complex traits, and functional significance of exonic single nucleotide polymorphisms
PLoS ONE
6
e26509
2011
Homo sapiens (P09172)
brenda
Kato, K.; Fushuku, S.; Yamamoto, Y.
Age-related changes in immunoreactivity for dopamine beta-hydroxylase in carotid body glomus cells in spontaneously hypertensive rats
Auton. Neurosci.
205
50-56
2017
Rattus norvegicus (Q05754), Rattus norvegicus Wistar Kyoto (Q05754)
brenda
Xu, Q.; Song, Y.; Liu, R.; Chen, Y.; Zhang, Y.; Li, Y.; Zhao, W.; Chang, G.; Chen, G.
The dopamine beta-hydroxylase gene in Chinese goose (Anas cygnoides) cloning, characterization, and expression during the reproductive cycle
BMC Genet.
17
48
2016
Anser cygnoides domesticus (A0A140GN70)
brenda
Kim, S.; Park, J.; Moon, J.; Choi, H.
Alpha-synuclein interferes with cAMP/PKA-dependent upregulation of dopamine beta-hydroxylase and is associated with abnormal adaptive responses to immobilization stress
Exp. Neurol.
252
63-74
2014
Homo sapiens (P09172), Mus musculus (Q64237)
brenda
Cheng, W.; Ka, Y.W.; Chang, C.C.
Dopamine beta-hydroxylase participate in the immunoendocrine responses of hypothermal stressed white shrimp, Litopenaeus vannamei
Fish Shellfish Immunol.
59
166-178
2016
Penaeus vannamei (A0A1I9LDK0), Penaeus vannamei
brenda
Cheng, W.; Ka, Y.W.; Chang, C.C.
Involvement of dopamine beta-hydroxylase in the neuroendocrine-immune regulatory network of white shrimp, Litopenaeus vannamei
Fish Shellfish Immunol.
68
92-101
2017
Penaeus vannamei (A0A1I9LDK0), Penaeus vannamei
brenda
Punchaichira, T.J.; Dey, S.K.; Mukhopadhyay, A.; Kundu, S.; Thelma, B.K.
Characterization of SNPs in the dopamine-beta-hydroxylase gene providing new insights into its structure-function relationship
Neurogenetics
18
155-168
2017
Homo sapiens (P09172)
brenda
Vendelboe, T.V.; Harris, P.; Zhao, Y.; Walter, T.S.; Harlos, K.; El Omari, K.; Christensen, H.E.
The crystal structure of human dopamine beta-hydroxylase at 2.9 A resolution
Sci. Adv.
2
e1500980
2016
Homo sapiens (P09172)
brenda
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