Information on EC 1.14.17.1 - dopamine beta-monooxygenase

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The expected taxonomic range for this enzyme is: Coelomata

EC NUMBER
COMMENTARY
1.14.17.1
-
RECOMMENDED NAME
GeneOntology No.
dopamine beta-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
show the reaction diagram
mechanism
-
dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
show the reaction diagram
stoichiometry
-
dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
show the reaction diagram
ping pong mechanism
-
dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
show the reaction diagram
uni-uni bi-uni ping pong mechanism
-
dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
show the reaction diagram
new mechanism of enzyme
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
catecholamine biosynthesis
-
-
catecholamine biosynthesis
-
-
Metabolic pathways
-
-
Tyrosine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
3,4-dihydroxyphenethylamine,ascorbate:oxygen oxidoreductase (beta-hydroxylating)
A copper protein. Stimulated by fumarate.
SYNONYMS
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
-
-
DbetaM
-
-
DBH
P09172
-
Dopa beta-hydroxylase
-
-
-
-
dopamine beta hydroxylase
E9JGS5
-
dopamine beta-hydrolase
-
-
-
-
dopamine beta-hydroxylase
-
-
-
-
dopamine beta-hydroxylase
-
-
dopamine beta-hydroxylase
-
-
dopamine beta-hydroxylase
-
-
dopamine beta-hydroxylase
-
-
dopamine beta-hydroxylase
P09172
-
dopamine beta-hydroxylase
-
-
dopamine beta-hydroxylase
-
-
dopamine beta-mono-oxygenase
-
-
dopamine beta-monooxygenase
-
-
dopamine beta-oxidase
-
-
-
-
dopamine hydroxylase
-
-
-
-
dopamine(3,4-dihydroxyphenethylamine)beta-mono-oxygenase
-
-
-
-
dopamine-B-hydroxylase
-
DBH
dopamine-beta hydroxylase
-
-
dopamine-beta-hydroxylase
-
-
dopamine-beta-hydroxylase
-
-
dopamine-beta-hydroxylase
-
-
dopamine-beta-monooxygenase
-
-
EC 1.14.2.1
-
-
formerly
-
MDBH
-
membrane-associated dopamine beta-monooxygenase
oxygenase, dopamine beta-mono-
-
-
-
-
pDbetaH
-
-
phenylamine beta-hydroxylase
-
-
-
-
plasma DbetaH activity
-
-
plasma dopamine beta-hydroxylase
-
-
plDbetaH
-
-
SDBH
-
soluble dopamine beta-monooxygenase
tyramine beta-monooxygenase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9013-38-1
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
tyramine beta-monooxygenase is homologous to mammalian dopamine beta-monooxygenase, tighter regulation of neurotransmitter levels by the insect enzyme than in the mammalian homologue
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-(4-hydroxybenzyl)imidazole + ascorbate + O2
4-hydroxybenzaldehyde + dehydroascorbate + H2O + ?
show the reaction diagram
-
-
-
?
1-(4-hydroxybenzyl)imidazole + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
1-phenyl-1-aminomethylethene + ascorbate + O2
2,3-dihydroxy-2-phenylpropylamine + dehydroascorbate + H2O + ?
show the reaction diagram
-
ascorbate and ferrocyanide can function as a electron donors
-
?
2-(4-hydroxyphenyl)prop-2-enylamine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
2-aminoindane + ascorbate + O2
trans-(1S,2S)-2-amino-1-indanol + H2O
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
2-chlorophenethylamine + ascorbate + O2
2-amino-1-chloro-1-phenylethanol + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
2-hydroxyphenethylamine + ascorbate + O2
2-amino-1-phenylethane-1,1-diol + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
2-phenylethylamine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
2-phenylprop-2-enylamine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
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
show the reaction diagram
-
ferrocyanide can function as a electron donor
norepinephrine
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
D-xyloascorbic acid, L-araboascorbic acid or D-araboascorbic acid can replace L-xyloascorbic acid
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
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
show the reaction diagram
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
-
?
3-phenylpropylamine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
-
3-phenylpropylamine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-hydroxy-alpha-methylstyrene + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-hydroxybenzyl cyanide + ascorbate + O2
4-hydroxymandelonitrile + dehydroascorbate + H2O
show the reaction diagram
-
and benzyl cyanide analogs
-
?
4-hydroxyphenyl-2-aminoethyl sulfide + ascorbate + O2
4-hydroxyphenyl-2-aminoethyl sulfoxide + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
4-hydroxyphenyl-2-aminopropyl selenide + ascorbate + O2
4-hydroxyphenyl-2-aminopropyl selenoxide + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
beta,beta-dideuterated tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
P09172
-
-
-
?
N-phenylethylenediamine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
octopamine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
phenyl 2-aminoethyl sulfide + ascorbate + O2
phenyl-2-aminoethyl sulfoxide + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
phenyl 2-aminoethyl sulfide + ascorbate + O2
phenyl-2-aminoethyl sulfoxide + dehydroascorbate + H2O
show the reaction diagram
-
and derivates
-
?
phenylacetaldehyde + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
phenylethylamine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
tyramine + ascorbate + ferrocyanide
octopamine + dehydroascorbate + ?
show the reaction diagram
-
-
-
-
?
tyramine + ascorbate + N,N,N',N'-tetramethyl-p-phenylenediamine
octopamine + dehydroascorbate + ?
show the reaction diagram
-
-
-
-
?
tyramine + ascorbate + N,N-dimethyl-p-phenylenediamine
octopamine + dehydroascorbate + ?
show the reaction diagram
-
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
tyramine + ascorbate + O2
octopamine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
tyramine + N-(4-chlorophenyl)-N'-hydroxyguanidine + O2
octopamine + 1-(4-chlorophenyl)urea + (4-chlorophenyl)cyanamide + 1-oxo-2-(4-chlorophenyl)guanidine + H2O
show the reaction diagram
-
-
-
-
?
tyramine + N-(4-isopropylphenyl)-N'-hydroxyguanidine + O2
octopamine + 1-(4-isopropylphenyl)urea + (4-isopropylphenyl)cyanamide + 1-oxo-2-(4-isopropylphenyl)guanidine + H2O
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
tyramine + N-(4-methylphenyl)-N'-hydroxyguanidine + O2
octopamine + 1-(4-methylphenyl)urea + (4-methylphenyl)cyanamide + 1-oxo-2-(4-methylphenyl)guanidine + H2O
show the reaction diagram
-
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
show the reaction diagram
-
16% of the activity with N-(4-methoxyphenyl)-N-hydroxyguanidine
-
-
?
dopamine + ascorbate + O2
norepinephrine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme with very broad substrate specifity
-
-
-
additional information
?
-
-
evidence that dioxygen and substrate activation are tightly coupled in dopamine beta-monooxygenase
-
-
-
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
?
-
-
a noradrenalin-synthesizing enzyme from dopamine
-
-
-
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
?
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
?
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
-
enzyme plays a key role in the biosynthetic interconversion of neurotransmitters
-
-
?
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
P09172
-
-
-
?
dopamine + ascorbate + O2
norepinephrine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
copper
P09172
contains copper
Cu2+
-
about 8 Cu2+ per tetramer; a copper protein
Cu2+
-
4 atoms of tightly bound copper per tetramer
Cu2+
-
a copper protein
Cu2+
-
a copper protein; 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+
-
-
Cu2+
-
3 mol of copper per mol of tetramer, MW 290000; a copper protein
Cu2+
-
Km: 0.00003-0.0002 mM
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; a copper protein
Cu2+
-
enzyme not activated by exogenous copper but activity decreases at high concentrations
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+
-
The enzyme contains two copper centers, one performs the substrate hydroxylation, while the second is used for electron storage/transfer
Cu2+
-
tyramine can bind to either the Cu(I) or Cu(II) forms of TbetaM
Fe2+
-
0.0004 mM per mol of enzyme
VO2+
-
1 VO2+/subunits during catalysis
Mg2+
-
regulates the translation of enzyme and affects the ratio of the two glycosylated forms of the enzyme
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1H)-Imidazole-4-acetic acid
-
-
1(2H)-Phthalazine hydrazone
-
hydralazine
1-(3,4-Dihydroxybenzyl)imidazole
-
-
1-(4-Hydroxybenzyl)-2-methylimidazole
-
-
1-(4-Hydroxybenzyl)imidazole
-
-
1-(4-Hydroxybenzyl)imidazole-2-thiol
-
-
1-(4-Hydroxybenzyl)pyrazole
-
-
1-(4-hydroxyphenyl)-1-(aminomethyl)-ethene
-
-
1-Benzimidazole
-
-
1-Benzylimidazole
-
-
1-Isoquinolinecarboxylic acid
-
-
1-Methylimidazole-2-thiol
-
-
1-Phenyl-1-aminomethylethene
-
suicide inhibition
1-Phenylpropene
-
-
2(1H)-Pyridinone hydrazone
-
2-hydrazinopyridine
2,2'-Bi-(1H)-imidazole
-
2,2'-biimidazole
2-(4-Hydroxyphenyl)prop-2-enylamine
-
-
2-Bromo-3-(p-hydroxyphenyl)-1-propene
-
mechanism-based inhibition
2-chlorophenethylamine
-
-
2-hydroxyphenylacetaldehyde
-
-
2-Phenylprop-2-enylamine
-
-
3-Phenylpropene
-
-
4-Hydroxy-alpha-methylstyrene
-
-
4-hydroxybenzaldehyde
-
-
4-Hydroxybenzyl cyanide
-
-
ascorbate
-
-
ascorbate
-
-
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
ascorbic acid oxidase
-
-
-
Bathocuproine disulfonate
-
-
beta,beta-difluorophenethylamine
-
weak competitive inhibitor
beta-Ethynyltyramine
-
and enantiomers, mechanism of inhibition
CaNa2EDTA
-
weak
-
catechol
-
-
CN-
-
-
diethyldicarbonate
-
-
diethyldithiocarbamate
-
-
Disulfiram
-
-
ferrocyanide
-
-
histidine
-
-
hydroquinone
-
-
N-ethylaniline
-
-
N-Phenylethylenediamine
-
-
N3-
-
-
Na2SO3
-
-
nepicastat
P09172
-
norepinephrine
-
-
p-Cresol
-
mechanism of inhibition
p-Cresol
-
-
p-Hydroxyphenylacetamide
-
-
phenylacetaldehyde
-
-
phenylacetamide
-
-
Quinoline-2-carboxylic acid
-
-
Sodium diethyldithiocarbamate
-
-
tyramine
-
rate of ascorbate reduction of the E-Cu(II) form of TbetaM is also reduced at high tyramine
malonate
-
-
additional information
-
suicide inactivation by benzyl cyanides
-
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
-
additional information
-
Cu deficiency limits DBM activity in vivo
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetate
-
-
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
ascorbic acid
-
complete dependance on added ascorbate, e.g. isoascorbate, glucoascorbate, D-ascorbate
cAMP
-
non-hydrolysable cAMP analog stimulates DBH promoter activity
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
-
dehydroascorbate
-
-
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
fumarate
-
-
fumarate
-
-
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.45
1-(4-chlorophenyl)-3-hydroxyguanidine
-
5 mM tyramine
1.9
1-(4-Hydroxybenzyl)imidazole
-
-
2.8
1-hydroxy-3-(4-methoxyphenyl)guanidine
-
pH 6.0, 28C, 0.4 mM tyramine
4.3
1-hydroxy-3-(4-methoxyphenyl)guanidine
-
pH 6.0, 28C, 1.0 mM tyramine
7.2
1-hydroxy-3-(4-methoxyphenyl)guanidine
-
pH 6.0, 28C, 5.0 mM tyramine
8.3
1-Phenyl-1-aminomethylethene
-
-
1.3
2-(4-Hydroxyphenyl)prop-2-enylamine
-
-
3.8
2-aminoindane
-
37C, 0.2 M acetate buffe, pI 6, with 30 mM NEM, 1 mM K4Fe(CN)6, 5 mM CuSO4
5.9
2-Bromo-3-(p-hydroxyphenyl)-1-propene
-
-
5.1
2-chlorophenethylamine
-
-
24
2-hydroxyphenethylamine
-
-
6.7
2-Phenylprop-2-enylamine
-
-
1
3,4-Dihydroxyphenethylamine
-
-
12.2
3-Phenylpropylamine
-
-
20.4
3-Phenylpropylamine
-
-
3.7
4-Hydroxy-alpha-methylstyrene
-
-
1.6
4-Hydroxybenzyl cyanide
-
-
0.6
ascorbate
-
in the absence of Cu2+
0.8
ascorbate
-
-
0.93
ascorbate
-
at 0.05 mM tyramine, pH 6 and 35C
1
ascorbate
-
in the presence of Cu2+
1.1
ascorbate
-
with or without Cu2+
1.1
ascorbate
-
-
1.25
ascorbate
-
-
1.98
ascorbate
-
at 0.1 mM tyramine, pH 6 and 35C
2
ascorbate
-
-
5.6
ascorbate
-
at 0.3 mM tyramine, pH 6 and 35C
6
ascorbate
-
-
16
ascorbate
-
at 0.7 mM tyramine, pH 6 and 35C
0.0906
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.907 mM O2, pH 6 and 35C
0.145
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.395 mM O2, pH 6 and 35C
0.177
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.119 mM O2, pH 6 and 35C
0.178
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.215 mM O2, pH 6 and 35C
0.193
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 1.039 mM O2, pH 6 and 35C
0.203
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.587 mM O2, pH 6 and 35C
0.231
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.056 mM O2, pH 6 and 35C
0.233
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.907 mM O2, pH 6 and 35C
0.245
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.214 mM O2, pH 6 and 35C
0.257
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.110 mM O2, pH 6 and 35C
0.316
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.598 mM O2, pH 6 and 35C
0.328
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.416 mM O2, pH 6 and 35C
0.341
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.063 mM O2, pH 6 and 35C
1.4
D-araboascorbic acid
-
-
2.3
D-xyloascorbic acid
-
-
0.2
dopamine
-
-
2.7
L-araboascorbic acid
-
-
9.1
N-Phenylethylenediamine
-
-
0.14
O2
-
in presence of tyramine
2.8
O2
-
in the presence of p-hydroxybenzyl cyanide
14
Octopamine
-
-
7.4
phenylacetaldehyde
-
-
7.9
phenylacetaldehyde
-
-
17.2
Phenylaminoethyl sulfide
-
-
-
26.5
Phenylaminoethyl sulfide
-
-
-
7
Phenylethylamine
-
-
0.0252
tyramine
-
at 2 mM ascorbate, pH 6 and 35C
0.0876
tyramine
-
at 10 mM ascorbate, 0.212 mM O2, pH 6 and 35C
0.088
tyramine
-
at 10 mM ascorbate, pH 6 and 35C
0.094
tyramine
-
at 10 mM ascorbate, 0.058 mM O2, pH 6 and 35C
0.096
tyramine
-
at 4 mM ascorbate, pH 6 and 35C
0.0976
tyramine
-
at 10 mM ascorbate, 1.04 mM O2, pH 6 and 35C
0.098
tyramine
-
at 10 mM ascorbate, 0.512 mM O2, pH 6 and 35C
0.113
tyramine
-
at 10 mM ascorbate, 0.103 mM O2, pH 6 and 35C
0.159
tyramine
-
at 10 mM ascorbate, 0.885 mM O2, pH 6 and 35C
0.188
tyramine
-
at 50 mM ascorbate, 0.059 mM O2, pH 6 and 35C
0.215
tyramine
-
at 50 mM ascorbate, 0.099 mM O2, pH 6 and 35C
0.23
tyramine
-
at 50 mM ascorbate, 1.04 mM O2, pH 6 and 35C
0.235
tyramine
-
at 50 mM ascorbate, 0.214 mM O2, pH 6 and 35C; at 50 mM ascorbate, pH 6 and 35C
0.242
tyramine
-
at 50 mM ascorbate, 0.395 mM O2, pH 6 and 35C
0.256
tyramine
-
at 50 mM ascorbate, 0.608 mM O2, pH 6 and 35C
0.265
tyramine
-
at 200 mM ascorbate, pH 6 and 35C
0.367
tyramine
-
at 100 mM ascorbate, pH 6 and 35C
0.387
tyramine
-
at 50 mM ascorbate, 0.854 mM O2, pH 6 and 35C
0.5 - 2
tyramine
-
enzyme from serum of 5-weeks-old rats, at 37C, pH not specified in the publication
0.55
tyramine
-
-
0.79
tyramine
-
enzyme from serum of 2-weeks-old rats, at 37C, pH not specified in the publication
0.92
tyramine
-
enzyme from serum of 8-weeks-old rats, at 37C, pH not specified in the publication
1.22
tyramine
-
enzyme from serum of 1-weeks-old rats, at 37C, pH not specified in the publication
1.3
tyramine
-
-
1.37
tyramine
-
enzyme from serum of 12-weeks-old rats, at 37C, pH not specified in the publication
1.6
tyramine
-
enzyme from serum of 15-weeks-old rats, at 37C, pH not specified in the publication
1.66
tyramine
-
deglycosylated enzyme
2
tyramine
-
-
2
tyramine
-
-
2
tyramine
-
-
2.1
tyramine
-
enzyme from serum of 27-weeks-old rats, at 37C, pH not specified in the publication
2.17
tyramine
-
native enzyme
2.3
tyramine
-
-
1.5
L-xyloascorbic acid
-
-
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
-
Km of N,N-dimethyl-1,4-phenylenediamine and ascorbic acid derivatives
-
additional information
additional information
-
comparison of Km of native enzyme and dimeric and tetrameric species after treatment with dithiothreitol and iodoacetamide
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.5
1-(4-Hydroxybenzyl)imidazole
-
-
10
1-Phenyl-1-aminomethylethene
-
-
65
1-Phenylethylamine
-
-
56
2-(4-hydroxphenyl)prop-2-enylamine
-
-
0.223
2-Bromo-3-(p-hydroxyphenyl)-1-propene
-
-
1.1
2-chlorophenethylamine
-
-
4.2
2-hydroxyphenethylamine
-
-
14
2-Phenylprop-2-enylamine
-
-
12
3-Phenylpropylamine
-
-
20.4
3-Phenylpropylamine
-
-
0.7
4-Hydroxy-alpha-methylstyrene
-
-
13
dopamine
-
-
110
dopamine
-
-
21
N-Phenylethylenediamine
-
-
33
Octopamine
-
-
1.7
phenylacetaldehyde
-
-
39
Phenylaminoethyl sulfide
-
-
-
68
Phenylaminoethyl sulfide
-
-
-
121
tyramine
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.55
ascorbate
-
at 0.7 mM tyramine, pH 6 and 35C
94
0.8
ascorbate
-
at 0.3 mM tyramine, pH 6 and 35C
94
1.14
ascorbate
-
at 0.1 mM tyramine, pH 6 and 35C
94
1.38
ascorbate
-
at 0.05 mM tyramine, pH 6 and 35C
94
4.95
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.056 mM O2, pH 6 and 35C
2802
5.8
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.063 mM O2, pH 6 and 35C
2802
9.6
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.110 mM O2, pH 6 and 35C
2802
10.9
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.119 mM O2, pH 6 and 35C
2802
13.5
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.214 mM O2, pH 6 and 35C
2802
14.3
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.215 mM O2, pH 6 and 35C
2802
19.4
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.395 mM O2, pH 6 and 35C; at 50 mM ascorbate, 0.416 mM O2, pH 6 and 35C
2802
20.1
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.587 mM O2, pH 6 and 35C
2802
24.6
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.598 mM O2, pH 6 and 35C
2802
29.2
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.907 mM O2, pH 6 and 35C
2802
38.6
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 1.039 mM O2, pH 6 and 35C
2802
39.4
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.907 mM O2, pH 6 and 35C
2802
15.4
tyramine
-
at 50 mM ascorbate, 0.059 mM O2, pH 6 and 35C
280
20.7
tyramine
-
at 10 mM ascorbate, 0.058 mM O2, pH 6 and 35C
280
25.5
tyramine
-
at 10 mM ascorbate, 0.103 mM O2, pH 6 and 35C
280
27.2
tyramine
-
at 50 mM ascorbate, 0.099 mM O2, pH 6 and 35C
280
31.9
tyramine
-
at 200 mM ascorbate, pH 6 and 35C
280
32.4
tyramine
-
at 100 mM ascorbate, pH 6 and 35C
280
33
tyramine
-
at 4 mM ascorbate, pH 6 and 35C
280
37.8
tyramine
-
at 50 mM ascorbate, 0.214 mM O2, pH 6 and 35C; at 50 mM ascorbate, pH 6 and 35C
280
44.7
tyramine
-
at 10 mM ascorbate, 0.212 mM O2, pH 6 and 35C
280
45
tyramine
-
at 10 mM ascorbate, pH 6 and 35C
280
47.7
tyramine
-
at 50 mM ascorbate, 0.395 mM O2, pH 6 and 35C
280
48.2
tyramine
-
at 50 mM ascorbate, 0.854 mM O2, pH 6 and 35C
280
52
tyramine
-
at 2 mM ascorbate, pH 6 and 35C
280
58.1
tyramine
-
at 10 mM ascorbate, 0.512 mM O2, pH 6 and 35C
280
58.6
tyramine
-
at 50 mM ascorbate, 0.608 mM O2, pH 6 and 35C
280
61.7
tyramine
-
at 10 mM ascorbate, 0.885 mM O2, pH 6 and 35C
280
70
tyramine
-
at 50 mM ascorbate, 1.04 mM O2, pH 6 and 35C
280
74.3
tyramine
-
at 10 mM ascorbate, 1.04 mM O2, pH 6 and 35C
280
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0057
1(2H)-Phthalazine hydrazone
-
-
4.6
1-(3,4-Dihydroxybenzyl)imidazole
-
-
2.9
1-(4-Hydroxybenzyl)-2-methylimidazole
-
-
0.16
1-(4-Hydroxybenzyl)pyrazole
-
-
11.9
1-Benzylimidazole
-
-
0.0009
1-Isoquinolinecarboxylic acid
-
-
0.8
1-Isoquinolinecarboxylic acid
-
-
13
1-Phenyl-1-aminomethylethene
-
-
2.5
1-Phenylpropene
-
-
0.0019
2(1H)-Pyridinone hydrazone
-
-
0.021
2,2'-Bi-(1H)-imidazole
-
-
0.52
2-(4-Hydroxyphenyl)prop-2-enylamine
-
-
4.9
2-Bromo-3-(p-hydroxyphenyl)-1-propene
-
-
4.7
2-Phenylprop-2-enylamine
-
-
3.6
3-Phenylpropene
-
-
2.5
4-Hydroxy-alpha-methylstyrene
-
-
2.3
4-hydroxybenzaldehyde
-
-
0.0011
ascorbate
-
at 0.05 mM tyramine, pH 6 and 35C
0.0018
ascorbate
-
at 0.1 mM tyramine, pH 6 and 35C
20
ascorbate
-
-
1.25
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.587 mM O2, pH 6 and 35C
2
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.907 mM O2, pH 6 and 35C
2.1
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.215 mM O2, pH 6 and 35C
2.4
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.395 mM O2, pH 6 and 35C
2.8
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.119 mM O2, pH 6 and 35C; at 50 mM ascorbate, 0.416 mM O2, pH 6 and 35C
2.86
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 1.039 mM O2, pH 6 and 35C
3.3
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.598 mM O2, pH 6 and 35C
3.35
beta,beta-dideuterated tyramine
-
at 10 mM ascorbate, 0.056 mM O2, pH 6 and 35C
4
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.907 mM O2, pH 6 and 35C
6
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.110 mM O2, pH 6 and 35C
7.4
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.063 mM O2, pH 6 and 35C
7.8
beta,beta-dideuterated tyramine
-
at 50 mM ascorbate, 0.214 mM O2, pH 6 and 35C
26
beta,beta-difluorophenethylamine
-
pH 6.0, 35C
0.015
beta-ethynytyramine
-
R,S-1
-
0.057
beta-ethynytyramine
-
S-1, in the presence of ascorbate
-
0.208
beta-ethynytyramine
-
S-1
-
0.41
histidine
-
-
0.37
hydroquinone
-
pH: 4.9
6.8
N-ethylaniline
-
-
1.1
N-Phenylethylenediamine
-
-
5
norepinephrine
-
-
0.14
Quinoline-2-carboxylic acid
-
-
0.98
tyramine
-
at 10 mM ascorbate, 0.885 mM O2, pH 6 and 35C
1.23
tyramine
-
at 10 mM ascorbate, 1.04 mM O2, pH 6 and 35C
1.3
tyramine
-
at 4 mM ascorbate, pH 6 and 35C
1.57
tyramine
-
at 50 mM ascorbate, 0.854 mM O2, pH 6 and 35C
1.9
tyramine
-
at 50 mM ascorbate, 0.608 mM O2, pH 6 and 35C
2.03
tyramine
-
at 50 mM ascorbate, 1.04 mM O2, pH 6 and 35C
2.07
tyramine
-
at 10 mM ascorbate, 0.512 mM O2, pH 6 and 35C
2.1
tyramine
-
at 2 mM ascorbate, pH 6 and 35C
2.46
tyramine
-
at 50 mM ascorbate, 0.395 mM O2, pH 6 and 35C
3.33
tyramine
-
at 10 mM ascorbate, 0.103 mM O2, pH 6 and 35C
3.5
tyramine
-
at 10 mM ascorbate, 0.212 mM O2, pH 6 and 35C; at 10 mM ascorbate, pH 6 and 35C
3.6
tyramine
-
at 100 mM ascorbate, pH 6 and 35C
3.97
tyramine
-
at 50 mM ascorbate, 0.099 mM O2, pH 6 and 35C
4.15
tyramine
-
at 50 mM ascorbate, 0.214 mM O2, pH 6 and 35C; at 50 mM ascorbate, pH 6 and 35C
7.82
tyramine
-
at 10 mM ascorbate, 0.058 mM O2, pH 6 and 35C
10.2
tyramine
-
at 50 mM ascorbate, 0.059 mM O2, pH 6 and 35C
10.3
tyramine
-
at 200 mM ascorbate, pH 6 and 35C
1.05
hydroquinone
-
pH: 5.9
additional information
additional information
-
-
-
additional information
additional information
-
KI as function of pH and fumarate activation
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.25
-
-
3.9
-
-
additional information
-
-
additional information
-
-
additional information
-
activity in the cat is twofold higher compared to rat
additional information
-
-
additional information
-
enzyme activity in plasma from combat veterans with or without chronic posttraumatic stress disorder, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.8 - 5
-
-
5 - 6
-
-
5
-
pI: 5.8
6
-
for the ferrocyanide as the sole electron donor
6
-
without anion activation or reaction with N,N,N,N-tetramethyl-p-phenylenediamine activated with 0.6 M Cl-
additional information
-
pI: 6.6 in the presence of 8 M urea
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.23
E9JGS5
theoretical
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
dietary copper deficiency is associated with increased formation of enzyme
Manually annotated by BRENDA team
-
dopamine beta-hydroxyase is reduced in rats subjected to chronic mild stress for 5 weeks. Imipramine treatment minimizes these chronic mild stress-induced reductions
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
highest activity
Manually annotated by BRENDA team
-
primary culture of trunk region of quail eggs, overview
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
lowest level of all tissues
Manually annotated by BRENDA team
-
a 75% decrease of dopamine-beta-hydroxyase expression is observed in rats exposed to 2,4-dichlorophenoxyacetic acid through lactation for 14 days
Manually annotated by BRENDA team
-
axons expressing dopamine beta hydroxyase frequenty made appositions to sympathetic and parasympathetic preganglionic neurons
Manually annotated by BRENDA team
-
neurons in primary neural crest stem cell culture
Manually annotated by BRENDA team
-
enzyme activity in plasma from combat veterans with or without chronic posttraumatic stress disorder, non-normal distribution, overview
Manually annotated by BRENDA team
-
neuroblastoma cell line
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
DBM protein is present in Cu-negative samples but not in Cu-positive samples
Manually annotated by BRENDA team
additional information
-
immunohistochemic localization analysis, overview
Manually annotated by BRENDA team
additional information
-
medulla oblongata/pons
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
recombinant enzyme
Manually annotated by BRENDA team
-
recombinant enzyme
-
Manually annotated by BRENDA team
-
the soluble enzyme form may not have access to the substrate
-
Manually annotated by BRENDA team
-
the membranous enzyme may be the physiologically functional form
Manually annotated by BRENDA team
additional information
-
enzyme-immunoreactive cells in anterior tuberal nucleus, locus coeruleus and caudal rhombencephalon
-
Manually annotated by BRENDA team
additional information
-
enzyme is studied in chromaffin granule ghosts: channeling of dopamine between monoamine transporter and membranous dopamine-beta-monooxygenase
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75000
-
Western blot analysis
702945
220000 - 250000
-
220000 Da, L208 homoenzyme, 230000 Da, F208 homoenzyme, 250000 Da, F208/L208 heteroenzyme, low-angle laser light scattering-photometry
438634
260000
-
native enzyme, low-angle laser light scattering photometry coupled with high-performance gel filtration
438629
280000
-
SDS-PAGE with 0.01% SDS
438604
290000
-
sedimentation equilibrium analysis, 5 mM potassium phosphate buffer, pH 6.8, 0.1 M NaCl
438599, 438608
290000
-
-
438623
300000
-
-
438600
300000
-
dimeric form, SDS-PAGE
438602
316000
-
gel filtration
438603
370000
-
in 5% ammonium sulfate buffer
438598
450000
-
in 0.2 M NaCl
438598
600000
-
in 1 M NaCl
438598
610000
-
tetrameric form, SDS-PAGE
438602
800000
-
in 5 mM sodium phosphate buffer, pH 7.0
438598
additional information
-
molecular forms change depending on concentration of salts and kind of salts
438598
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 75000, SDS-PAGE of reduced and carboxymethylated MDBH
?
-
x * 70000-75000, Western blot analysis, recombinant enzyme
?
E9JGS5
x * 68480, predicted
?
-
x * 72000, secreted and modified (N-glycosylation) form, Western blot analysis
tetramer
-
4 * 88000 SDS-PAGE
tetramer
-
4 * 80000, SDS-PAGE after treatment with 2-mercaptoethanol, subunits joined in pairs by disulfide bonds
tetramer
-
4 * 65000, deduced from cDNA
tetramer
-
4 * 72000 SDS-PAGE
tetramer
-
4 * 66000-74000, SDS-PAGE after cleavage of intersubunit disulfide bonds with dithiothreitol, tetramer consists of two disulfid-linked dimers
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
oligosaccharide moieties do not play a role in catalysis
glycoprotein
-
3.5 residues of glucosamine per subunit, glucosamine is the only hexosamine detected
glycoprotein
-
5% carbohydrate by weight
phospholipoprotein
-
hypothesis: completely processed enzyme may be anchored to cellular membranes by binding to phosphatidylserine
glycoprotein
-
-
glycoprotein
-
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 4
-
24 h, 10-15% loss of activity
438603
50
-
4 h, about 10% loss of activity
438624
60
-
2 h, about 30% loss of activity
438624
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and subsequent thawing results in rapid decrease of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-30C, 10 mM potassium phosphate buffer, pH 6.5, stable for at least 1 month
-
0-4C, 10-15% loss of activity in 24 h
-
4C, stable for at least several days, dimeric species
-
-20C, stable for at least 6 weeks
-
4C, 0.5 M NaCl in 0.02 M sodium phosphate, pH 7.0, several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
large scale
-
partial
-
partially, from adrenal medulla after crude extract PEG 6000 precipitation and DEAE-Sepharose chromatography
-
recombinant enzyme
-
by anion exchange and His tag affinity chromatography, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Drosophila Schneider 2 cells
-
expressed in Escherichia coli TOP10F'
E9JGS5
gene DBH, DNA and amino acid sequence determination and analysis, expression of the GST-tagged enzyme in Escherichia coli strain BL21 (DE3)
-
TbetaM expressed in Drosophila Schneider 2 (S2) 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, genotyping, overview
-
myc-tagged version expressed in CHO cell
-
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
-
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
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
-
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
-
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
-
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
-
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
-
enzyme expression is highest in 5-weeks-old rats
-
ENGINEERING
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
P09172
the mutation does not influence enzyme activity
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
G482R
P09172
the mutation has subsequent effect on the activity of the enzyme as it is present close to the active site
L317P
P09172
the mutation does not influence enzyme activity
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
R549C
P09172
the mutation causes abnormal oligomerization through non-native disulfide bond formation
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
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
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
-
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
-
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
-
adequate dietary Cu is essential to support DBM function in vivo
medicine
-
the antidepressant drug imipramine counteracts the chronic mild stress-induced reduction of plasma dopamine beta-hydroxylase activity
medicine
-
adequate dietary Cu is essential to support DBM function in vivo