National Center for
2YP1: Crystallization Of A 45 Kda Peroxygenase- Peroxidase From The Mushroom Agrocybe Aegerita And Structure Determination By Sad Utilizing Only The Haem Iron
Structural basis of substrate conversion in a new aromatic peroxygenase: cytochrome P450 functionality with benefits
J. Biol. Chem. (2013) 288 p.34767-34776» All references (2)
Aromatic peroxygenases (APOs) represent a unique oxidoreductase sub-subclass of heme proteins with peroxygenase and peroxidase activity and were thus recently assigned a distinct EC classification (EC 22.214.171.124). They catalyze, inter alia, oxyfunctionalization reactions of aromatic and aliphatic hydrocarbons with remarkable regio- and stereoselectivities. When compared with cytochrome P450, APOs appear to be the choice enzymes for oxyfunctionalizations in organic synthesis due to their independence from a cellular environment and their greater chemical versatility. Here, the first two crystal structures of a heavily glycosylated fungal aromatic peroxygenase (AaeAPO) are described. They reveal different pH-dependent ligand binding modes. We model the fitting of various substrates in AaeAPO, illustrating the way the enzyme oxygenates polycyclic aromatic hydrocarbons. Spatial restrictions by a phenylalanine pentad in the active-site environment govern substrate specificity in AaeAPO.