Dopamine beta-monooxygenase

In enzymology, a dopamine beta-monooxygenase 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.