Dopamine beta-monooxygenase

Dopamine beta-monooxygenase
dopamine beta-monooxygenase
Identifiers
EC number 1.14.17.1
CAS number 9013-38-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

In enzymology, a dopamine beta-monooxygenase (EC 1.14.17.1) is an enzyme that catalyzes the chemical reaction

3,4-dihydroxyphenethylamine + ascorbate + O2 \rightleftharpoons noradrenaline + dehydroascorbate + H2O

The 3 substrates of this enzyme are 3,4-dihydroxyphenethylamine, ascorbate, and O2, whereas its 3 products are noradrenaline, dehydroascorbate, and H2O.

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with reduced ascorbate as one donor, and incorporation of one ato of oxygen into the other donor. The systematic name of this enzyme class is 3,4-dihydroxyphenethylamine,ascorbate:oxygen oxidoreductase (beta-hydroxylating). Other names in common use include dopamine beta-hydroxylase, MDBH (membrane-associated dopamine beta-monooxygenase), SDBH (soluble dopamine beta-monooxygenase), dopamine-B-hydroxylase, oxygenase, dopamine beta-mono-, 3,4-dihydroxyphenethylamine beta-oxidase, 4-(2-aminoethyl)pyrocatechol beta-oxidase, dopa beta-hydroxylase, dopamine beta-oxidase, dopamine hydroxylase, phenylamine beta-hydroxylase, and (3,4-dihydroxyphenethylamine)beta-mono-oxygenase. This enzyme participates in tyrosine metabolism. It has 3 cofactors: copper, PQQ, and Fumarate.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1ZHB.

References

  • Friedman S, Kaufman S (1965). "3,4-dihydroxyphenylethylamine beta-hydroxylase. Physical properties, copper content, and role of copper in the catalytic acttivity". J. Biol. Chem. 240 (12): 4763–73. PMID 5846992. 
  • Levin EY, Levenberg B and Kaufman S (1960). "The enzymatic conversion of 3,4-dihydroxyphenylethylamine to norepinephrine". J. Biol. Chem. 235: 2080–2086. 
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