Aromatic Peroxygenase Structures

by David

Aromatic peroxygenases have catalytic activity similar to that of cytochrome P450 monoxygenases (hydroxylation, S-oxidation, N-oxidation) on both aromatic and aliphatic substrates.  Unlike P450
monooxygenases, these enzymes have no need for NAD(P)H and complicated reductase domains and instead use hydrogen peroxide as the oxidant. The aromatic peroxygenase from the edible commercial mushroom, Agrocybe aegerita, is one of the well-studied enzymes of this class, and all of the known aromatic peroxygenases occur in fungi.  Piontek, Plattner, and co-workers have solved two crystal structures of this aromatic peroxygenase, and these structures help to explain its unique
properties.  Thanks to a vigilant reader for bringing this research to our attention, which can be found at:
http://www.jbc.org/content/288/48/34767.abstract  (‘Structural Basis of Substrate Conversion in a New Aromatic Peroxygenase: Cytochrome P450 functionality with benefits’)

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