2yor

Publication Abstract from PubMed

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 1.11.2.1). They catalyze, inter alia, oxyfunctionalization reactions of aromatic and aliphatic hydrocarbons with remarkable regio and stereoselectivities. 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 (PAHs). Spatial restrictions by a phenylalanine pentad in the active-site environment govern substrate specificity in AaeAPO.

Structural Basis of Substrate Conversion in a New Aromatic Peroxygenase: P450 Functionality with Benefits.,Piontek K, Strittmatter E, Ullrich R, Grobe G, Pecyna MJ, Kluge M, Scheibner K, Hofrichter M, Plattner DA J Biol Chem. 2013 Oct 14. PMID:24126915^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.