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- W2015342817 abstract "Publisher Summary This chapter describes the serum dopamine 3-hydroxylase (DBH) as an index of sympathetic function. DBH is a copper-containing mixed function oxidase that catalysis hydroxylation of the three carbon in the side chain of phenylethylamine derivatives. The enzyme has been tentatively characterized as a tetrameric glycoprotein with 1 or 2 active sites, each containing one copper molecule that undergoes cyclic oxidation and reduction. It has a molecular weight of close to 290,000. Under dissociating conditions, four subunits of molecular weight 75,000 have been reported but it is uncertain whether the units are identical or catalytically active. Enzymatic activity may depend upon the cooperative action of two or even all four subunits, and upon sugar residues that comprise 4% of the molecule. Amino acid analysis has revealed that DBH is a highly acidic protein, rich in glutamate and aspartate, and deficient in methionine and half-cystine. The enzyme requires molecular oxygen and a reducing agent as cofactors. Ascorbate is generally used to reduce the enzyme in vitro but can be replaced by dimethyltetrahydropterine. Pterines may therefore play a similar regulatory role to that proposed in the first rate-limiting step in catecholamine synthesis catalyzed by tyrosine hydroxylase." @default.
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- W2015342817 title "Serum dopamine β-hydroxylase as an index of sympathetic function" @default.
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- W2015342817 doi "https://doi.org/10.1016/0024-3205(74)90262-8" @default.
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