The Copper-Enzyme Family of Dopamine β-Monooxygenase and Peptidylglycine α-Hydroxylating Monooxygenase: Resolving the Chemical Pathway for Substrate Hydroxylation*
By J. Klinman. Journal of Biological Chemistry, 2006
275 citations recorded by the source corpus.
Dopamine -monooxygenase (D M)2 and peptidylglycine -hydroxylating monooxygenase (PHM) belong to a small class of copper proteins found exclusively in higher eukaryotes. These physiologically important enzymes catalyze the transformation of dopamine to norepinephrine (D M) (Equation 1) and C-terminal glycine-extended peptides to their -hydroxylated products (PHM) (Equation 2). Although their substrate specificities are grossly different,
Subfields: Inorganic Chemistry, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/17f7776d08ae3dcc70f485c8f81a27691739641a
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In Inorganic Chemistry
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Citations in the corpus
- Biologically inspired oxidation catalysis (2008, background): “, dopamine β-monooxygenase (DβM) and peptidylglycine α-hydroxylating monooxygenase (PHM”