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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

Reaction

dopamine
+ 2 ascorbate +
O2
=
noradrenaline
+ 2 monodehydroascorbate +
H2O

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 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.17 With reduced ascorbate as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.17.1 dopamine beta-monooxygenase

Activating Compound

Activating Compound on EC 1.14.17.1 - dopamine beta-monooxygenase

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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