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 hide
1.14.17.1
-
RECOMMENDED NAME
GeneOntology No.
dopamine beta-monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dopamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
catecholamine biosynthesis
Metabolic pathways
-
-
Tyrosine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
3,4-dihydroxyphenethylamine,ascorbate:oxygen oxidoreductase (beta-hydroxylating)
A copper protein. Stimulated by fumarate.
CAS REGISTRY NUMBER
COMMENTARY hide
9013-38-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
gene DBH
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-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
norepinephrine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
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
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 + 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
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3,4-dihydroxyphenethylamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
dopamine + ascorbate + O2
noradrenaline + dehydroascorbate + H2O
show the reaction diagram
P09172
-
-
-
?
dopamine + ascorbate + O2
norepinephrine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
contains copper
Fe2+
-
0.0004 mM per mol of enzyme
Mg2+
-
regulates the translation of enzyme and affects the ratio of the two glycosylated forms of the enzyme
VO2+
-
1 VO2+/subunits during catalysis
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 hide
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
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
-
-
malonate
-
-
N-ethylaniline
-
-
N-Phenylethylenediamine
-
-
N3-
-
-
Na2SO3
-
-
nepicastat
-
norepinephrine
-
-
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
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
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
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 hide
LITERATURE
IMAGE
0.45
1-(4-chlorophenyl)-3-hydroxyguanidine
-
5 mM tyramine
1.9
1-(4-Hydroxybenzyl)imidazole
-
-
2.8 - 7.2
1-hydroxy-3-(4-methoxyphenyl)guanidine
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 - 20.4
3-Phenylpropylamine
3.7
4-Hydroxy-alpha-methylstyrene
-
-
1.6
4-Hydroxybenzyl cyanide
-
-
0.6 - 16
ascorbate
0.0906 - 0.341
beta,beta-dideuterated tyramine
1.4
D-araboascorbic acid
-
-
2.3
D-xyloascorbic acid
-
-
0.2
dopamine
-
-
2.7
L-araboascorbic acid
-
-
1.5
L-xyloascorbic acid
-
-
9.1
N-Phenylethylenediamine
-
-
0.14 - 2.8
O2
14
octopamine
-
-
7.4 - 7.9
phenylacetaldehyde
17.2 - 26.5
Phenylaminoethyl sulfide
7
Phenylethylamine
-
-
0.0252 - 2.3
tyramine
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.5
1-(4-Hydroxybenzyl)imidazole
Bos taurus
-
-
10
1-Phenyl-1-aminomethylethene
Bos taurus
-
-
65
1-Phenylethylamine
Bos taurus
-
-
56
2-(4-hydroxphenyl)prop-2-enylamine
Bos taurus
-
-
0.223
2-Bromo-3-(p-hydroxyphenyl)-1-propene
Bos taurus
-
-
1.1
2-chlorophenethylamine
Bos taurus
-
-
4.2
2-hydroxyphenethylamine
Bos taurus
-
-
14
2-Phenylprop-2-enylamine
Bos taurus
-
-
12 - 20.4
3-Phenylpropylamine
0.7
4-Hydroxy-alpha-methylstyrene
Bos taurus
-
-
13 - 110
dopamine
21
N-Phenylethylenediamine
Bos taurus
-
-
33
octopamine
Bos taurus
-
-
1.7
phenylacetaldehyde
Bos taurus
-
-
39 - 68
Phenylaminoethyl sulfide
121
tyramine
Bos taurus
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.55 - 1.38
ascorbate
4.95 - 39.4
beta,beta-dideuterated tyramine
15.4 - 74.3
tyramine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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 - 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 - 20
ascorbate
1.25 - 7.8
beta,beta-dideuterated tyramine
26
beta,beta-difluorophenethylamine
-
pH 6.0, 35C
0.015 - 0.208
beta-ethynytyramine
0.41
histidine
-
-
0.37 - 1.05
hydroquinone
6.8
N-ethylaniline
-
-
1.1
N-Phenylethylenediamine
-
-
5
norepinephrine
-
-
0.14
Quinoline-2-carboxylic acid
-
-
0.98 - 10.3
tyramine
additional information
additional information
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.25
-
-
3.9
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8 - 5
-
-
5 - 6
-
-
5
-
pI: 5.8
additional information
-
pI: 6.6 in the presence of 8 M urea
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.23
theoretical
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
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
-
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
-
SH-SY5Y-AH1861
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
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
280000
-
SDS-PAGE with 0.01% SDS
290000
300000
316000
-
gel filtration
370000
-
in 5% ammonium sulfate buffer
450000
-
in 0.2 M NaCl
600000
-
in 1 M NaCl
610000
-
tetrameric form, SDS-PAGE
800000
-
in 5 mM sodium phosphate buffer, pH 7.0
additional information
-
molecular forms change depending on concentration of salts and kind of salts
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
phospholipoprotein
-
hypothesis: completely processed enzyme may be anchored to cellular membranes by binding to phosphatidylserine
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 4
-
24 h, 10-15% loss of activity
50
-
4 h, about 10% loss of activity
60
-
2 h, about 30% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and subsequent thawing results in rapid decrease of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 6 weeks
-
-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, 0.5 M NaCl in 0.02 M sodium phosphate, pH 7.0, several weeks
-
4C, stable for at least several days, dimeric species
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by anion exchange and His tag affinity chromatography, and gel filtration
-
large scale
-
partial
-
partially, from adrenal medulla after crude extract PEG 6000 precipitation and DEAE-Sepharose chromatography
-
recombinant enzyme
-
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)
-
expressed in Escherichia coli TOP10F'
expression in AtT-20 corticotrope tumor cells, PC12 pheochromocytoma cells and Chinese hamster ovary cells
-
expression in Drosophila Schneider 2 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
-
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
-
myc-tagged version expressed in CHO cell
-
TbetaM expressed in Drosophila Schneider 2 (S2) cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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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
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enzyme expression is highest in 5-weeks-old rats
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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
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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
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
the mutation does not influence enzyme activity
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
G482R
the mutation has subsequent effect on the activity of the enzyme as it is present close to the active site
L317P
the mutation does not influence enzyme activity
R549C
the mutation causes abnormal oligomerization through non-native disulfide bond formation
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diagnostics
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genotype-controlled measurement of plasma DBH activity might be used as a potential biological marker of the response to trauma
medicine