1.14.17.1: dopamine beta-monooxygenase
This is an abbreviated version!
For detailed information about dopamine beta-monooxygenase, go to the full flat file.
Word Map on EC 1.14.17.1
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1.14.17.1
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catecholamine
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noradrenergic
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norepinephrine
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nerve
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sympathetic
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noradrenaline
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adrenal
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innervation
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medulla
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fiber
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dopaminergic
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neuropeptide
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chromaffin
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adrenergic
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monoamine
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neurotransmitter
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ganglia
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coeruleus
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hypothalamus
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catecholaminergic
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phenylethanolamine
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npy
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epinephrine
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cholinergic
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adrenaline
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phenylethanolamine-n-methyltransferase
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n-methyltransferase
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varicosity
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vasoactive
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rostrally
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reserpine
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gene-related
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catecholamine-synthesizing
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disulfiram
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peptidylglycine
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preganglionic
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adrenomedullary
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th-immunoreactive
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orthostatic
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preoptic
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ventrolateral
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monoaminergic
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parabrachial
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saporin
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intermediolateral
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hydroxylase-immunoreactive
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cytoarchitectonic
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medicine
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drug development
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postrema
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diagnostics
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histofluorescence
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alpha-methyl-p-tyrosine
- 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
Reaction
Synonyms
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, DBM, Dopa beta-hydroxylase, dopamine beta hydroxylase, dopamine beta-hydrolase, 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, dopamine-beta hydroxylase, dopamine-beta-hydroxylase, dopamine-beta-monooxygenase, EC 1.14.2.1, gDBH, LvDBH, MDBH, oxygenase, dopamine beta-mono-, pDbetaH, phenylamine beta-hydroxylase, plasma DbetaH activity, plasma dopamine beta-hydroxylase, plDbetaH, SDBH, TBetaM, tyramine beta-monooxygenase
ECTree
1.14.17.1 dopamine beta-monooxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.14.17.1 - dopamine beta-monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L208F
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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
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retained inside cell in a premature endoplasmic reticulum form, also naturally occuring mutation
C1021T
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naturally occuring gene polymorphism, determination of the frequency in combat veterans with or without chronic posttraumatic stress disorder, overview
D100E
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retained inside cell in a premature endoplasmic reticulum form, also naturally occuring mutation
D331N
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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
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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
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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
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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
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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
