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 (Metals Ions
Metals Ions on EC 1.14.17.1 - dopamine beta-monooxygenase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cu2+
Mg2+
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regulates the translation of enzyme and affects the ratio of the two glycosylated forms of the enzyme
additional information
Cu2+
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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+
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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+
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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+
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tyramine can bind to either the Cu(I) or Cu(II) forms of TbetaM
Cu2+
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enzyme not activated by exogenous copper but activity decreases at high concentrations
Cu2+
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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+
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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
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Cu2+, Mn2+, Ni2+, Co2+, Zn2+, Pb2+, Fe2+, Fe3+ reduce translation of enzyme at concentrations above 1.5 mM, Ni2+ and Cu2+ inhibit the glycosylation
